Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(ethylsulfinyl)benzene + reduced benzyl viologen
(ethylsulfanyl)benzene + H2O + oxidized benzyl viologen
(methylsulfinyl)benzene + reduced benzyl viologen
(methylsulfanyl)benzene + H2O + oxidized benzyl viologen
(propan-2-ylsulfinyl)benzene + reduced benzyl viologen
(propan-2-ylsulfanyl)benzene + H2O + oxidized benzyl viologen
(propylsulfanyl)benzene + reduced benzyl viologen
(propylsulfinyl)benzene + H2O + oxidized benzyl viologen
(R)-ethyl 2-pyridyl sulfoxide + reduced methyl viologen + H2O
ethyl 2-pyridyl sulfide + oxidized methyl viologen
(R)-methoxymethyl phenyl sulfoxide + reduced methyl viologen + H2O
methoxymethyl phenyl sulfide + oxidized methyl viologen
(R)-methyl p-tolyl sulfoxide + reduced methyl viologen + H2O
methyl p-tolyl sulfide + oxidized methyl viologen
(R)-methylthiomethyl methyl sulfoxide + reduced methyl viologen + H2O
methylthiomethyl methyl sulfide + oxidized methyl viologen
(S)-ethyl 2-pyridyl sulfoxide + reduced methyl viologen + H2O
ethyl 2-pyridyl sulfide + oxidized methyl viologen
-
-
-
-
?
(S)-methoxymethyl phenyl sulfoxide + reduced methyl viologen + H2O
methoxymethyl phenyl sulfide + oxidized methyl viologen
-
-
-
-
?
(S)-methyl p-tolyl sulfoxide + reduced methyl viologen + H2O
methyl p-tolyl sulfide + oxidized methyl viologen
-
catalyses the selective removal of (S)-methyl p-tolyl sulfoxide from a racemic mixture of methyl p-tolyl sulfoxide, resulting in an 88 O/o recovery of enantiomerically pure (R)-methyl p-tolyl sulfoxide
-
-
?
(S)-methylthiomethyl methyl sulfoxide + reduced methyl viologen + H2O
methylthiomethyl methyl sulfide + oxidized methyl viologen
-
-
-
-
?
1-bromo-4-(methylsulfinyl)benzene + reduced benzyl viologen
1-bromo-4-(methylsulfanyl)benzene + H2O + oxidized benzyl viologen
-
180% of the rate with dimethysulfoxide
-
-
?
1-methyl-4-(methylsulfinyl)benzene + reduced benzyl viologen
1-methyl-4-(methylsulfanyl)benzene + H2O + oxidized benzyl viologen
-
150% of the rate with dimethysulfoxide
-
-
?
2-carboxypyridine N-oxide + reduced benzyl viologen + H2O
2-carboxypyridine + oxidized benzyl viologen
-
-
-
-
?
2-chloropyridine N-oxide + reduced benzyl viologen + H2O
2-chloropyridine + oxidized benzyl viologen
-
-
-
-
?
2-hydroxymethylpyridine N-oxide + reduced benzyl viologen + H2O
2-hydroxymethylpyridine + oxidized benzyl viologen
-
-
-
-
?
2-mercaptopyridine N-oxide + reduced benzyl viologen + H2O
2-mercaptopyridine + oxidized benzyl viologen
-
-
-
-
?
2-methylpyridine N-oxide + reduced benzyl viologen + H2O
2-methylpyridine + oxidized benzyl viologen
-
-
-
-
?
3-amidopyridine N-oxide + reduced benzyl viologen + H2O
3-amidopyridine + oxidized benzyl viologen
-
-
-
-
?
3-carboxypyridine N-oxide + reduced benzyl viologen + H2O
3-carboxypyridine + oxidized benzyl viologen
-
-
-
-
?
3-hydroxymethylpyridine N-oxide + reduced benzyl viologen + H2O
3-hydroxymethylpyridine + oxidized benzyl viologen
-
-
-
-
?
3-hydroxypyridine N-oxide + reduced benzyl viologen + H2O
3-hydroxypyridine + oxidized benzyl viologen
-
-
-
-
?
3-methylpyridine N-oxide + reduced benzyl viologen + H2O
3-methylpyridine + oxidized benzyl viologen
-
-
-
-
?
3alpha-hydroxybenzylpyridine N-oxide + reduced benzyl viologen + H2O
3alpha-hydroxybenzylpyridine + oxidized benzyl viologen
-
-
-
-
?
4-carboxypyridine N-oxide + reduced benzyl viologen + H2O
4-carboxypyridine + oxidized benzyl viologen
-
-
-
-
?
4-chloropyridine N-oxide + reduced benzyl viologen + H2O
4-chloropyridine + oxidized benzyl viologen
-
-
-
-
?
4-hydroxymethylpyridine N-oxide + reduced benzyl viologen + H2O
4-hydroxymethylpyridine + oxidized benzyl viologen
-
-
-
-
?
4-methylmorpholine N-oxide + reduced benzyl viologen + H2O
4-methylmorpholine + oxidized benzyl viologen
-
-
-
-
?
4-methylpyridine N-oxide + reduced benzyl viologen + H2O
4-methylpyridine + oxidized benzyl viologen
-
-
-
-
?
4-phenylpyridine N-oxide + reduced benzyl viologen + H2O
4-phenylpyridine + oxidized benzyl viologen
-
-
-
-
?
adenosine-1N-oxide + reduced dichlorophenolindophenol
adenine + H2O + oxidized dichlorophenolindophenol
-
-
-
-
r
dimethyl sulfoxide + reduced methyl viologen
dimethyl sulfide + H2O + oxidized methyl viologen
-
-
-
r
dimethyldodecylamine N-oxide + reduced benzyl viologen + H2O
dimethyldodecylamine + oxidized benzyl viologen
-
-
-
-
?
dimethylsulfide + H2O + oxidized benzyl viologen
dimethylsulfoxide + reduced benzyl viologen
-
-
-
-
r
dimethylsulfide + H2O + oxidized methyl viologen
dimethylsulfoxide + reduced methyl viologen
-
-
-
-
r
dimethylsulfide + H2O + pyridine N-oxide
dimethylsulfoxide + pyridine
-
-
-
-
?
dimethylsulfide + menaquinone + H2O
dimethylsulfoxide + menaquinol
-
-
-
?
dimethylsulfoxide + 2,3-dimethyl-1,4-naphthoquinol
dimethylsulfide + H2O + 2,3-dimethyl-1,4-naphthoquinone
-
-
-
-
r
dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
dimethylsulfoxide + methyl viologen
dimethylsulfide + oxidized methyl viologen + H2O
dimethylsulfoxide + reduced benzyl viologen
dimethylsulfide + H2O + oxidized benzyl viologen
dimethylsulfoxide + reduced benzyl viologen + H2O
dimethylsulfide + oxidized benzyl viologen
-
-
-
-
?
dimethylsulfoxide + reduced dichlorophenolindophenol
dimethylsulfide + H2O + oxidized dichlorophenolindophenol
-
-
-
-
r
dimethylsulfoxide + reduced methyl viologen
dimethylsulfide + H2O + oxidized methyl viologen
-
-
-
-
r
dithane 1-oxide + reduced benzyl viologen + H2O
dithane + oxidized benzyl viologen
-
-
-
-
?
DL-methionine sulfoxide + menaquinol
DL-methionine sulfide + menaquinone + H2O
DL-methyl phenyl sulfoxide + reduced benzyl viologen + H2O
DL-methyl phenyl sulfide + oxidized benzyl viologen
-
-
-
-
?
methionine sulfoxide + reduced benzyl viologen + H2O
methionine + oxidized benzyl viologen
-
-
-
-
?
methionine sulfoxide + reduced dichlorophenolindophenol
methionine + H2O + oxidized dichlorophenolindophenol
-
-
-
-
r
pyridine N-oxide + reduced benzyl viologen + H2O
pyridine + oxidized benzyl viologen
-
-
-
-
?
S-biotin sulfoxide + menaquinol
S-biotin sulfide + menaquinone + H2O
tetramethylene sulfoxide + reduced benzyl viologen + H2O
tetramethylene sulfide + oxidized benzyl viologen
-
-
-
-
?
trimethylamine N-oxide + reduced benzyl viologen
trimethylamine + oxidized benzyl viologen
-
-
-
?
trimethylamine N-oxide + reduced benzyl viologen + H2O
trimethylamine + oxidized benzyl viologen
-
-
-
-
?
trimethylamine N-oxide + reduced dichlorophenolindophenol
trimethylamine + H2O + oxidized dichlorophenolindophenol
-
-
-
-
r
trimethylamine N-oxide + reduced lapachol
trimethylamine + oxidized lapachol
-
-
-
?
trimethylamine-N-oxide + menaquinol
? + menaquinone + H2O
trimethylamine-N-oxide + reduced methyl viologen
trimethylamine + H2O + oxidized methyl viologen
-
-
-
-
r
[(methylsulfinyl)methyl]benzene + reduced benzyl viologen
[(methylsulfanyl)methyl]benzene + H2O + oxidized benzyl viologen
-
130% of the rate with dimethysulfoxide
-
-
?
additional information
?
-
(ethylsulfinyl)benzene + reduced benzyl viologen
(ethylsulfanyl)benzene + H2O + oxidized benzyl viologen
-
90% of the rate with dimethysulfoxide
-
-
?
(ethylsulfinyl)benzene + reduced benzyl viologen
(ethylsulfanyl)benzene + H2O + oxidized benzyl viologen
Cereibacter sphaeroides f.s. denitrificans
-
90% of the rate with dimethysulfoxide
-
-
?
(methylsulfinyl)benzene + reduced benzyl viologen
(methylsulfanyl)benzene + H2O + oxidized benzyl viologen
-
150% of the rate with dimethysulfoxide
-
-
?
(methylsulfinyl)benzene + reduced benzyl viologen
(methylsulfanyl)benzene + H2O + oxidized benzyl viologen
Cereibacter sphaeroides f.s. denitrificans
-
150% of the rate with dimethysulfoxide
-
-
?
(propan-2-ylsulfinyl)benzene + reduced benzyl viologen
(propan-2-ylsulfanyl)benzene + H2O + oxidized benzyl viologen
-
35% of the rate with dimethysulfoxide
-
-
?
(propan-2-ylsulfinyl)benzene + reduced benzyl viologen
(propan-2-ylsulfanyl)benzene + H2O + oxidized benzyl viologen
Cereibacter sphaeroides f.s. denitrificans
-
35% of the rate with dimethysulfoxide
-
-
?
(propylsulfanyl)benzene + reduced benzyl viologen
(propylsulfinyl)benzene + H2O + oxidized benzyl viologen
-
35% of the rate with dimethysulfoxide
-
-
?
(propylsulfanyl)benzene + reduced benzyl viologen
(propylsulfinyl)benzene + H2O + oxidized benzyl viologen
Cereibacter sphaeroides f.s. denitrificans
-
35% of the rate with dimethysulfoxide
-
-
?
(R)-ethyl 2-pyridyl sulfoxide + reduced methyl viologen + H2O
ethyl 2-pyridyl sulfide + oxidized methyl viologen
-
-
-
-
?
(R)-ethyl 2-pyridyl sulfoxide + reduced methyl viologen + H2O
ethyl 2-pyridyl sulfide + oxidized methyl viologen
-
-
-
-
?
(R)-ethyl 2-pyridyl sulfoxide + reduced methyl viologen + H2O
ethyl 2-pyridyl sulfide + oxidized methyl viologen
-
-
-
-
?
(R)-methoxymethyl phenyl sulfoxide + reduced methyl viologen + H2O
methoxymethyl phenyl sulfide + oxidized methyl viologen
-
-
-
-
?
(R)-methoxymethyl phenyl sulfoxide + reduced methyl viologen + H2O
methoxymethyl phenyl sulfide + oxidized methyl viologen
-
-
-
-
?
(R)-methoxymethyl phenyl sulfoxide + reduced methyl viologen + H2O
methoxymethyl phenyl sulfide + oxidized methyl viologen
-
-
-
-
?
(R)-methyl p-tolyl sulfoxide + reduced methyl viologen + H2O
methyl p-tolyl sulfide + oxidized methyl viologen
-
-
-
-
?
(R)-methyl p-tolyl sulfoxide + reduced methyl viologen + H2O
methyl p-tolyl sulfide + oxidized methyl viologen
-
-
-
-
?
(R)-methyl p-tolyl sulfoxide + reduced methyl viologen + H2O
methyl p-tolyl sulfide + oxidized methyl viologen
-
-
-
-
?
(R)-methylthiomethyl methyl sulfoxide + reduced methyl viologen + H2O
methylthiomethyl methyl sulfide + oxidized methyl viologen
-
-
-
-
?
(R)-methylthiomethyl methyl sulfoxide + reduced methyl viologen + H2O
methylthiomethyl methyl sulfide + oxidized methyl viologen
-
-
-
-
?
(R)-methylthiomethyl methyl sulfoxide + reduced methyl viologen + H2O
methylthiomethyl methyl sulfide + oxidized methyl viologen
-
-
-
-
?
dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
-
-
-
?
dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
-
-
-
-
?
dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
-
-
-
?
dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
-
-
-
?
dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
-
-
-
?
dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
-
-
-
?
dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
-
-
-
?
dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
-
-
-
?
dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
-
-
-
?
dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
-
-
-
?
dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
-
-
-
?
dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
-
-
-
?
dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
-
-
-
?
dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
-
-
-
?
dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
-
-
-
-
?
dimethylsulfoxide + menaquinol
dimethylsulfide + menaquinone + H2O
-
-
-
-
?
dimethylsulfoxide + methyl viologen
dimethylsulfide + oxidized methyl viologen + H2O
-
-
-
?
dimethylsulfoxide + methyl viologen
dimethylsulfide + oxidized methyl viologen + H2O
-
activity of mutant C176D of periplasmic nitrate reductase NapA (EC 1.9.6.1), no activity with wild-type NapA or C176S/A NapA mutants
-
-
?
dimethylsulfoxide + reduced benzyl viologen
dimethylsulfide + H2O + oxidized benzyl viologen
-
-
-
-
?
dimethylsulfoxide + reduced benzyl viologen
dimethylsulfide + H2O + oxidized benzyl viologen
-
-
-
-
r
dimethylsulfoxide + reduced benzyl viologen
dimethylsulfide + H2O + oxidized benzyl viologen
-
-
-
-
r
DL-methionine sulfoxide + menaquinol
DL-methionine sulfide + menaquinone + H2O
-
-
-
?
DL-methionine sulfoxide + menaquinol
DL-methionine sulfide + menaquinone + H2O
-
-
-
?
DL-methionine sulfoxide + menaquinol
DL-methionine sulfide + menaquinone + H2O
-
-
-
?
DL-methionine sulfoxide + menaquinol
DL-methionine sulfide + menaquinone + H2O
-
-
-
?
DL-methionine sulfoxide + menaquinol
DL-methionine sulfide + menaquinone + H2O
-
-
-
?
S-biotin sulfoxide + menaquinol
S-biotin sulfide + menaquinone + H2O
-
-
-
?
S-biotin sulfoxide + menaquinol
S-biotin sulfide + menaquinone + H2O
-
-
-
?
S-biotin sulfoxide + menaquinol
S-biotin sulfide + menaquinone + H2O
-
-
-
?
S-biotin sulfoxide + menaquinol
S-biotin sulfide + menaquinone + H2O
-
-
-
?
S-biotin sulfoxide + menaquinol
S-biotin sulfide + menaquinone + H2O
-
-
-
?
trimethylamine-N-oxide + menaquinol
? + menaquinone + H2O
-
-
-
?
trimethylamine-N-oxide + menaquinol
? + menaquinone + H2O
-
-
-
?
trimethylamine-N-oxide + menaquinol
? + menaquinone + H2O
-
-
-
?
trimethylamine-N-oxide + menaquinol
? + menaquinone + H2O
-
-
-
?
trimethylamine-N-oxide + menaquinol
? + menaquinone + H2O
-
-
-
?
additional information
?
-
-
for all substrates studied, enzyme catalyzes deoxygenation of (S)-sulfoxides predominantly
-
-
?
additional information
?
-
Cereibacter sphaeroides f.s. denitrificans
-
for all substrates studied, enzyme catalyzes deoxygenation of (S)-sulfoxides predominantly
-
-
?
additional information
?
-
-
enzyme catalyses the enantioselective reduction of (R)-sulfoxides
-
-
?
additional information
?
-
-
for the reduction of dimethylsulfoxide, NADH, formate, lactate, reduced benzyl viologen, reduced methyl viologen, and dithionite can serve as electron donors. Menaquinone is involved in electron transport during dimethylsulfoxide reduction
-
-
?
additional information
?
-
-
enzyme catalyses the enantioselective reduction of (R)-sulfoxides
-
-
?
additional information
?
-
-
enzyme catalyses the enantioselective reduction of (R)-sulfoxides
-
-
?
additional information
?
-
-
enzyme catalyses the enantioselective reduction of (S)-sulfoxides
-
-
?
additional information
?
-
formation of the intermediate formed by reaction of DMSOR with dimethylsulfide occurs at a redox potential that is 80 mV higher than that required for reduction of Mo(VI) to Mo(IV) in the free enzyme. In the back-assay the Mo(IV) state may at least in part be by-passed via two successive one electron-reactions of the intermediate with the electron-acceptor
-
-
?
additional information
?
-
-
formation of the intermediate formed by reaction of DMSOR with dimethylsulfide occurs at a redox potential that is 80 mV higher than that required for reduction of Mo(VI) to Mo(IV) in the free enzyme. In the back-assay the Mo(IV) state may at least in part be by-passed via two successive one electron-reactions of the intermediate with the electron-acceptor
-
-
?
additional information
?
-
-
Second-order rate constants for the two-electron reduction and reoxidation reactions at pH 5.5 are 190000 and 430 per M and s, respectively, while at pH 8.0, the catalytic step is rate-limiting. Kinetically, for the two-electron reactions, the enzyme is more effective in dimethylsulfide oxidation than in dimethylsulfoxide reduction. Reduction of DMSOR by dimethylsulfide is incomplete below 1 mM dimethylsulfide but complete at higher concentrations. Reoxidation of the dimethylsulfide-reduced state by dimethylsulfoxide is always incomplete
-
-
?
additional information
?
-
-
CymA, a cytoplasmic membrane-bound tetraheme c-type cytochrome, serves as a preferential electron transport protein for the type I and type VI DMSO reductases, in which type VI accepts electrons from CymA in a DmsE and DmsF-independent manner
-
-
-
additional information
?
-
-
CymA, a cytoplasmic membrane-bound tetraheme c-type cytochrome, serves as a preferential electron transport protein for the type I and type VI DMSO reductases, in which type VI accepts electrons from CymA in a DmsE and DmsF-independent manner
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
bis(molybdopterin guanine dinucleotide)molybdenum cofactor
molybdenum bis-molybdopterin guanine dinucleotide
molybdo-bis(pyranopterin guanine dinucleotide)
-
molybdopterin guanine dinucleotide
-
-
[4Fe-4S]-center
role for the cluster in directing molybdenum cofactor assembly during enzyme maturation. The cluster is predicted to be in close proximity to the molybdo-bis(pyranopterin guanine dinucleotide) cofactor, which provides the site of dimethyl sulfoxide reduction
bis(molybdopterin guanine dinucleotide)molybdenum cofactor
-
presence of a monooxo molybdenum cofactor containing two molybdopterin guanine dinucleotides that asymmetrically coordinate the molybdenum through their dithiolene groups. One of the pterins exhibits different coordination modes to the molybdenum between the oxidized and reduced states, whereas the side chain oxygen of Ser147 coordinates the metal in both states
bis(molybdopterin guanine dinucleotide)molybdenum cofactor
-
protein contains 1 mol of molybdenum, 4 mol of organic phosphate, and 2 mol of guanine per mole of protein
bis(molybdopterin guanine dinucleotide)molybdenum cofactor
-
the bis-molybdopterin guanine dinucleotide cofactor of the single chain protein has the molybdenum ion bound to the cis-dithiolene group of only one molybdopterin guanine dinucleotide molecule. Three additional ligands, two oxo groups and the oxygen of a serine side-chain, are bound to the molybdenum ion. The second molybdopterin system is not part of the ligand sphere of the metal center
Fe-S center
-
residues Pro80, Ser81, Cys102, and Tyr104 of electron transfer subunit DmsB are located at the DmsB-DmsC interface and are critical for the transfer of electrons from MQH2 to iron-sulfur cluster FS4
Fe-S center
-
significant spin-spin interaction between the reduced [4Fe-4S] cluster of subunit DmsB and the Mo(V) of the Mo-bisMGD of subunit DmsA. This interaction is significantly modified in a DmsA-C38S mutant that contains a [3Fe-4S] cluster in DmsA
methyl viologen
-
-
molybdenum bis-molybdopterin guanine dinucleotide
-
reaction profile for oxygen atom transfer from dimethylsulfoxide to [Mo(IV)(OMe)(S2C2H2)2]1- compared to the corresponding reaction with [W(IV)(OMe)(S2C2H2)2]1-. Both reaction profiles involve two transition states separated by a well-defined intermediate. The second transition state TS2 is clearly rate-limiting for the Mo system, and the two transition states have a similar energy for the W system. The activation energy for oxygen atom transfer from dimethylsulfoxide to [W(IV)(OMe)(S2C2H2)2]1- is ca. 23 kJ per mol lower for the corresponding reaction with Mo, consistent with the significantly faster rate of reduction of dimethylsulfoxide by Rhodobacter capsulatus W-dimethylsulfoxide reductase than by its Mo counterpart. The geometrical constraints imposed by the protein on the metal centre of the Mo- and W-dimethylsulfoxide reductases facilitate oxygen atom transfer by favouring a trigonal prismatic geometry for the transition state TS2 that is close to that observed for the metal in the oxidised form of each of these enzymes. The major effect of different tautomers of a simplified form of the pyran ring-opened, dihydropterin state, a significant lowering of the activation barrier associated with TS2, is observed for a protonated form of a tautomer that involves conjugation between the pyrazine and metallodithiolene rings
molybdenum bis-molybdopterin guanine dinucleotide
-
the molybdenum cofactor in dimethylsulfoxide reductase is bis(molybdopterin guanine dinucleotide) molybdenum. Protein contains 1 mol Mo and 2 mol GMP. Approximately 2 mol. electrons/2 mol molybdopterin guanine dinucleotide reduce 2,6-dichloroindophenol. Presence of one molybdopterin guanine dinucleotide moiety with a pyrazine ring at the oxidation level of a dihydropteridine and one molybdopterin guanine dinucleotide moiety with a pyrazine ring at the oxidation level of a fully aromatic pteridine
molybdenum cofactor
-
molybdenum cofactor
-
residue W116 forms a hydrogen bond with a single oxo ligand bound to the molybdenum ion. Mutation of this residue to phenylalanine affects the UV/visible spectrum of the purified MoVI form of dimethylsulfoxide reductase resulting in the loss of the characteristic transition at 720 nm. W116 plays a critical role in stabilizing the hexacoordinate monooxo MoVI form of the enzyme and prevents the formation of a dioxo pentacoordinate MoVI species
molybdenum cofactor
-
MoCo, the cofactor coordinates organic molybdopterin to molybdenum, over 50 different molybdopterin enzymes are known to catalyze a variety of chemistries in the cycling of C, N, S, As, and Se, all relying on the same basic cofactor, the MoCo. Kinetic consequences of the exchange of the endogenous ligand to molybdenum with other ligands within the cofactor of DMSO reductase family enzymes, overview. The mutant C176D of periplasmic nitrate reductase NapA (EC 1.9.6.1) is active with DMSO (and artificial cosubstrate methyl viologen), while the wild-type NapA is not
molybdenum cofactor
pterin-based cofactor MoCo, molybdenum is not active in cells until it forms the MoCo. The DMSO reductases family cofactor is the bis-molybdopterin-guanine dinucleotide (Bis-MGD) and it is composed by two pyranopterin molecules (instead of one pyranopterin as in sulfite oxidases and xanthine oxidases families), which are conjugated with nucleosides: cytosine or guanosine. In this family, the Mo atom in the MoCo is coordinated by four sulfur atoms of the pyranopterins rings and by an inorganic ion that could be selenium, oxygen, or sulfur atoms. In almost all cases, another ligand that has a role in coordination comes from an amino acid side chain that can be aspartate, serine, cysteine, and selenocysteine. Depending on this amino acid, the DMSO reductases can be classified in three types: cysteine or selenocysteine for type I, an aspartate for type II, and serine residue for type III. Enzyme DmsA is a type III enzyme
molybdenum cofactor
pterin-based cofactor MoCo, molybdenum is not active in cells until it forms the MoCo. The DMSO reductases family cofactor is the bis-molybdopterin-guanine dinucleotide (Bis-MGD) and it is composed by two pyranopterin molecules (instead of one pyranopterin as in sulfite oxidases and xanthine oxidases families), which are conjugated with nucleosides: cytosine or guanosine. In this family, the Mo atom in the MoCo is coordinated by four sulfur atoms of the pyranopterins rings and by an inorganic ion that could be selenium, oxygen, or sulfur atoms. In almost all cases, another ligand that has a role in coordination comes from an amino acid side chain that can be aspartate, serine, cysteine, and selenocysteine. Depending on this amino acid, the DMSO reductases can be classified in three types: cysteine or selenocysteine for type I, an aspartate for type II, and serine residue for type III. Enzyme DmsA is a type III enzyme. The Mo amino acid ligand in the MoCo of Halobacterium salinarum DmsA is an aspartate residue in all halophilic archaea instead of a serine residue
molybdenum cofactor
pterin-based cofactor MoCo, the unique cofactor contains the ligand pyranopterin ene-1,2-dithiolate. Mechanism for mature Moco formation, overview. Bacterial DMSO reductase family enzymes possess a bis-molybdopterin guanine dinucleotide (bis-MGD) cofactor that is obtained by adding GMP to the MPT terminal phosphates. Enzymes that belong to the DMSO reductase enzyme family possess two coordinated MPTs, with one of the MPTs adopting an SO family configuration and the other a more distorted XO enzyme family structure, role of MPT in catalysis
molybdenum cofactor
pterin-based cofactor MoCo, the unique cofactor contains the ligand pyranopterin ene-1,2-dithiolate. Mechanism for mature Moco formation, overview. Bacterial DMSO reductase family enzymes possess a bis-molybdopterin guanine dinucleotide (bis-MGD) cofactor that is obtained by adding GMP to the MPT terminal phosphates. Enzymes that belong to the DMSO reductase enzyme family possess two coordinated MPTs, with one of the MPTs adopting an SO family configuration and the other a more distorted XO enzyme family structure, role of MPT in catalysis
molybdenum cofactor
two desoxo molybdenum(V) complexes are synthesized and characterized as models for the paramagnetic high-g split intermediate observed in the catalytic cycle of dimethyl sulfoxide reductase (DMSOR), analysis of extended X-ray absorption fine structure (EXAFS) and electron paramagnetic resonance (EPR) data. A 6-coordinate [(PDT)2Mo(OH)(OSer)]- structure (PDT = pyranopterin dithiolene) is supported for a high-g split with four S donors from two PDT ligands, a coordinated hydroxyl ligand, and a serinate O donor. This geometry orients the redox orbital toward the substrate access channel for the two-electron reduction of substrates. Detailed overview
molybdenum cofactor
two desoxo molybdenum(V) complexes are synthesized and characterized as models for the paramagnetic high-g split intermediate observed in the catalytic cycle of dimethyl sulfoxide reductase (DMSOR), analysis of extended X-ray absorption fine structure (EXAFS) and electron paramagnetic resonance (EPR) data. A 6-coordinate [(PDT)2Mo(OH)(OSer)]- structure (PDT = pyranopterin dithiolene) is supported for a high-g split with four S donors from two PDT ligands, a coordinated hydroxyl ligand, and a serinate O donor. This geometry orients the redox orbital toward the substrate access channel for the two-electron reduction of substrates. Detailed overview
additional information
-
CymA serves as a preferential electron transport protein for the type I and type VI DMSO reductases, in which type VI accepts electrons from CymA in a DmsE- and DmsF-independent manner. DmsE passes electrons to DmsA1 for DMSO reduction. In-frame deletion mutagenesis of dmsE (swp3461) and analysis
-
additional information
kinetic and spectroscopic analysis of molybdenum-DMSO reductase and a tungsten-substituted form of DMSO reductase, overview. Partial reduction with sodium dithionite yields a well-resolved W(V) EPR signal of the so-called high-g split type that exhibits markedly greater g-anisotropy than the corresponding Mo(V) signal of the native form of the enzyme, with the g values shifted to higher magnetic field by as much as DELTAgave = 0.056. Deuteration of the enzyme confirms that the coupled proton is solvent-exchangeable, allowing to accurately simulate the tungsten hyperfine coupling. Global curve-fitting analysis of UV/vis absorption spectra observed in the course of the reaction of the tungsten-substituted enzyme with sodium dithionite affords a well-defined absorption spectrum for the W(V) species. The absorption spectrum for this species exhibits significantly larger molar extinction coefficients than either the reduced or the oxidized spectrum. This spectrum, in conjunction with those for fully oxidized W(VI) and fully reduced W(IV) enzyme, is used to deconvolute the absorption spectra seen in the course of turnover, in which the enzyme is reacted with sodium dithionite and DMSO, demonstrating that the W(V) is an authentic catalytic intermediate that accumulates to approximately 50% of the total enzyme in the steady state
-
additional information
-
kinetic and spectroscopic analysis of molybdenum-DMSO reductase and a tungsten-substituted form of DMSO reductase, overview. Partial reduction with sodium dithionite yields a well-resolved W(V) EPR signal of the so-called high-g split type that exhibits markedly greater g-anisotropy than the corresponding Mo(V) signal of the native form of the enzyme, with the g values shifted to higher magnetic field by as much as DELTAgave = 0.056. Deuteration of the enzyme confirms that the coupled proton is solvent-exchangeable, allowing to accurately simulate the tungsten hyperfine coupling. Global curve-fitting analysis of UV/vis absorption spectra observed in the course of the reaction of the tungsten-substituted enzyme with sodium dithionite affords a well-defined absorption spectrum for the W(V) species. The absorption spectrum for this species exhibits significantly larger molar extinction coefficients than either the reduced or the oxidized spectrum. This spectrum, in conjunction with those for fully oxidized W(VI) and fully reduced W(IV) enzyme, is used to deconvolute the absorption spectra seen in the course of turnover, in which the enzyme is reacted with sodium dithionite and DMSO, demonstrating that the W(V) is an authentic catalytic intermediate that accumulates to approximately 50% of the total enzyme in the steady state
-
additional information
tungsten is present as cofactor in tungsten enzymes, sharing a lot of resemblances with the MoCo of DMSO reductases
-
additional information
tungsten is present as cofactor in tungsten enzymes, sharing a lot of resemblances with the MoCo of DMSO reductases
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.043
2-chloropyridine N-oxide
-
pH 7.0, 30°C
0.092
2-methylpyridine N-oxide
-
pH 7.0, 30°C
0.045
3-amidopyridine N-oxide
-
pH 7.0, 30°C
4.94
3-carboxypyridine N-oxide
-
pH 7.0, 30°C
0.094
3-hydroxymethylpyridine N-oxide
-
pH 7.0, 30°C
3.17
3-hydroxypyridine N-oxide
-
pH 7.0, 30°C
0.089
3-methylpyridine N-oxide
-
pH 7.0, 30°C
0.158
3alpha-hydroxybenzylpyridine N-oxide
-
pH 7.0, 30°C
0.513
4-chloropyridine N-oxide
-
pH 7.0, 30°C
0.372
4-hydroxymethylpyridine N-oxide
-
pH 7.0, 30°C
11.1
4-methylmorpholine N-oxide
-
pH 7.0, 30°C
0.452
4-methylpyridine N-oxide
-
pH 7.0, 30°C
0.246
4-phenylpyridine N-oxide
-
pH 7.0, 30°C
0.02 - 0.52
adenosine-1N-oxide
0.83
dimethyldodecylamine N-oxide
-
pH 7.0, 30°C
0.007 - 0.4
Dimethylsulfoxide
0.21
DL-methyl phenyl sulfoxide
-
pH 7.0, 30°C
0.09 - 19
methionine sulfoxide
0.001 - 3.8
Pyridine N-oxide
0.001 - 1.1
reduced benzyl viologen
0.06
tetramethylene sulfoxide
-
pH 7.0, 30°C
2.3 - 88
Trimethylamine N-oxide
0.0959 - 0.193
Trimethylamine-N-oxide
additional information
additional information
-
0.02
adenosine-1N-oxide
-
wild-type, pH 8.0, temperature not specified in the publication
0.08
adenosine-1N-oxide
-
mutant Y114A, pH 8.0, temperature not specified in the publication
0.52
adenosine-1N-oxide
-
mutant Y114F, pH 8.0, temperature not specified in the publication
0.007
Dimethylsulfoxide
-
wild-type, pH 8.0, temperature not specified in the publication
0.0097
Dimethylsulfoxide
-
wild-type, pH not specified in the publication, temperature not specified in the publication
0.0261
Dimethylsulfoxide
-
mutant W116F, pH not specified in the publication, temperature not specified in the publication
0.0282
Dimethylsulfoxide
-
pH 6.0, 25°C, recombinant NapA mutant C176D
0.064
Dimethylsulfoxide
W-DMSOR, pH 6.0, temperature not specified in the publication
0.18
Dimethylsulfoxide
-
pH 7.0, 30°C
0.18
Dimethylsulfoxide
-
mutant Y114F, pH 8.0, temperature not specified in the publication
0.4
Dimethylsulfoxide
-
mutant Y114A, pH 8.0, temperature not specified in the publication
0.09
methionine sulfoxide
-
pH 7.0, 30°C
0.33
methionine sulfoxide
-
wild-type, pH 8.0, temperature not specified in the publication
16
methionine sulfoxide
-
mutant Y114A, pH 8.0, temperature not specified in the publication
19
methionine sulfoxide
-
mutant Y114F, pH 8.0, temperature not specified in the publication
0.001
Pyridine N-oxide
-
mutant A178Q, pH not specified in the publication, temperature not specified in the publication
0.024
Pyridine N-oxide
-
mutant T148S, pH not specified in the publication, temperature not specified in the publication
0.028
Pyridine N-oxide
-
mutant W357Y, pH not specified in the publication, temperature not specified in the publication
0.034
Pyridine N-oxide
-
mutant Q179I, pH not specified in the publication, temperature not specified in the publication
0.048
Pyridine N-oxide
-
mutant W191G, pH not specified in the publication, temperature not specified in the publication
0.048
Pyridine N-oxide
-
mutant W357F, pH not specified in the publication, temperature not specified in the publication
0.076
Pyridine N-oxide
-
mutant G167N, pH not specified in the publication, temperature not specified in the publication
0.094
Pyridine N-oxide
-
pH 7.0, 30°C
0.095
Pyridine N-oxide
-
mutant W357C, pH not specified in the publication, temperature not specified in the publication
0.1
Pyridine N-oxide
-
wild-type, pH not specified in the publication, temperature not specified in the publication
0.11
Pyridine N-oxide
-
mutant M147L, pH not specified in the publication, temperature not specified in the publication
0.12
Pyridine N-oxide
-
mutant G190V, pH not specified in the publication, temperature not specified in the publication
0.12
Pyridine N-oxide
-
mutant R149C, pH not specified in the publication, temperature not specified in the publication
0.14
Pyridine N-oxide
-
mutant G190D, pH not specified in the publication, temperature not specified in the publication
0.18
Pyridine N-oxide
-
mutant M147I, pH not specified in the publication, temperature not specified in the publication
0.24
Pyridine N-oxide
-
mutant A181T, pH not specified in the publication, temperature not specified in the publication
3.8
Pyridine N-oxide
-
mutant R217Q, pH not specified in the publication, temperature not specified in the publication
0.001
reduced benzyl viologen
-
mutant A178Q, pH not specified in the publication, temperature not specified in the publication
0.019
reduced benzyl viologen
-
mutant Q179I, pH not specified in the publication, temperature not specified in the publication
0.019
reduced benzyl viologen
-
mutant W357Y, pH not specified in the publication, temperature not specified in the publication
0.02
reduced benzyl viologen
-
mutant M147I, pH not specified in the publication, temperature not specified in the publication
0.023
reduced benzyl viologen
-
mutant W357F, pH not specified in the publication, temperature not specified in the publication
0.024
reduced benzyl viologen
-
mutant W357C, pH not specified in the publication, temperature not specified in the publication
0.028
reduced benzyl viologen
-
mutant W191G, pH not specified in the publication, temperature not specified in the publication
0.032
reduced benzyl viologen
-
wild-type, pH not specified in the publication, temperature not specified in the publication
0.033
reduced benzyl viologen
-
mutant G190V, pH not specified in the publication, temperature not specified in the publication
0.038
reduced benzyl viologen
-
mutant G167N, pH not specified in the publication, temperature not specified in the publication
0.038
reduced benzyl viologen
-
mutant G190D, pH not specified in the publication, temperature not specified in the publication
0.039
reduced benzyl viologen
-
mutant A181T, pH not specified in the publication, temperature not specified in the publication
0.04
reduced benzyl viologen
-
mutant M147L, pH not specified in the publication, temperature not specified in the publication
0.076
reduced benzyl viologen
-
mutant R149C, pH not specified in the publication, temperature not specified in the publication
0.11
reduced benzyl viologen
-
mutant T148S, pH not specified in the publication, temperature not specified in the publication
1.1
reduced benzyl viologen
-
mutant R217Q, pH not specified in the publication, temperature not specified in the publication
2.3
Trimethylamine N-oxide
-
mutant Y114A, pH 8.0, temperature not specified in the publication
20.2
Trimethylamine N-oxide
-
pH 7.0, 30°C
68
Trimethylamine N-oxide
-
wild-type, pH 8.0, temperature not specified in the publication
88
Trimethylamine N-oxide
-
mutant Y114F, pH 8.0, temperature not specified in the publication
0.0959
Trimethylamine-N-oxide
-
mutant W116F, pH not specified in the publication, temperature not specified in the publication
0.193
Trimethylamine-N-oxide
-
wild-type, pH not specified in the publication, temperature not specified in the publication
additional information
additional information
pre-steady-state kinetics and enzyme-monitored turnover, and steady-state kinetics, kinetic analysis of molybdenum-DMSO reductase and a tungsten-substituted form of DMSO reductase, overview
-
additional information
additional information
-
pre-steady-state kinetics and enzyme-monitored turnover, and steady-state kinetics, kinetic analysis of molybdenum-DMSO reductase and a tungsten-substituted form of DMSO reductase, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
8
2-carboxypyridine N-oxide
-
pH 7.0, 30°C
307
2-chloropyridine N-oxide
-
pH 7.0, 30°C
89.3
2-hydroxymethylpyridine N-oxide
-
pH 7.0, 30°C
8
2-mercaptopyridine N-oxide
-
pH 7.0, 30°C
247
2-methylpyridine N-oxide
-
pH 7.0, 30°C
237
3-amidopyridine N-oxide
-
pH 7.0, 30°C
168
3-carboxypyridine N-oxide
-
pH 7.0, 30°C
214
3-hydroxymethylpyridine N-oxide
-
pH 7.0, 30°C
429
3-hydroxypyridine N-oxide
-
pH 7.0, 30°C
231
3-methylpyridine N-oxide
-
pH 7.0, 30°C
229
3alpha-hydroxybenzylpyridine N-oxide
-
pH 7.0, 30°C
30.3
4-carboxypyridine N-oxide
-
pH 7.0, 30°C
212
4-chloropyridine N-oxide
-
pH 7.0, 30°C
226
4-hydroxymethylpyridine N-oxide
-
pH 7.0, 30°C
573
4-methylmorpholine N-oxide
-
pH 7.0, 30°C
268
4-methylpyridine N-oxide
-
pH 7.0, 30°C
297
4-phenylpyridine N-oxide
-
pH 7.0, 30°C
110 - 2200
adenosine-1N-oxide
21 - 470
dimethyl sulfoxide
239
dimethyldodecylamine N-oxide
-
pH 7.0, 30°C
8
Dimethylsulfide
-
pH 8.0, 25°C
0.023 - 1120
Dimethylsulfoxide
28.4
dithane 1-oxide
-
pH 7.0, 30°C
99.6
DL-methyl phenyl sulfoxide
-
pH 7.0, 30°C
58 - 180
methionine sulfoxide
14 - 370
reduced benzyl viologen
27
reduced methyl viologen
-
pH 8.0, 25°C
119
tetramethylene sulfoxide
-
pH 7.0, 30°C
1203 - 4300
Trimethylamine N-oxide
11.3 - 134.5
Trimethylamine-N-oxide
110
adenosine-1N-oxide
-
wild-type, pH 8.0, temperature not specified in the publication
1200
adenosine-1N-oxide
-
mutant Y114A, pH 8.0, temperature not specified in the publication
2200
adenosine-1N-oxide
-
mutant Y114F, pH 8.0, temperature not specified in the publication
21
dimethyl sulfoxide
enzyme Mo-DMSOR with molybdenum in the catalytic centre, pH not specified in the publication, temperature not specified in the publication
470
dimethyl sulfoxide
enzyme W-DMSOR with tungsten in the catalytic centre, pH not specified in the publication, temperature not specified in the publication
0.023
Dimethylsulfoxide
-
pH 6.0, 25°C, recombinant NapA mutant C176D
7
Dimethylsulfoxide
-
mutant W116F, pH not specified in the publication, temperature not specified in the publication
42.9
Dimethylsulfoxide
-
wild-type, pH not specified in the publication, temperature not specified in the publication
50
Dimethylsulfoxide
-
wild-type, pH 8.0, temperature not specified in the publication
67
Dimethylsulfoxide
-
mutant Y114A, pH 8.0, temperature not specified in the publication
79.9
Dimethylsulfoxide
-
pH 7.0, 30°C
180
Dimethylsulfoxide
-
mutant Y114F, pH 8.0, temperature not specified in the publication
1120
Dimethylsulfoxide
W-DMSOR, pH 6.0, temperature not specified in the publication
58
methionine sulfoxide
-
wild-type, pH 8.0, temperature not specified in the publication
61.1
methionine sulfoxide
-
pH 7.0, 30°C
92
methionine sulfoxide
-
mutant Y114A, pH 8.0, temperature not specified in the publication
180
methionine sulfoxide
-
mutant Y114F, pH 8.0, temperature not specified in the publication
3 - 6
Pyridine N-oxide
-
mutant Q179I, pH not specified in the publication, temperature not specified in the publication
10
Pyridine N-oxide
-
mutant A178Q, pH not specified in the publication, temperature not specified in the publication
33
Pyridine N-oxide
-
mutant W357Y, pH not specified in the publication, temperature not specified in the publication
41
Pyridine N-oxide
-
mutant W357F, pH not specified in the publication, temperature not specified in the publication
95
Pyridine N-oxide
-
mutant R149C, pH not specified in the publication, temperature not specified in the publication
96
Pyridine N-oxide
-
mutant T148S, pH not specified in the publication, temperature not specified in the publication
99
Pyridine N-oxide
-
mutant G167N, pH not specified in the publication, temperature not specified in the publication
99
Pyridine N-oxide
-
mutant W191G, pH not specified in the publication, temperature not specified in the publication
100
Pyridine N-oxide
-
mutant W357C, pH not specified in the publication, temperature not specified in the publication
110
Pyridine N-oxide
-
mutant M147L, pH not specified in the publication, temperature not specified in the publication
120
Pyridine N-oxide
-
mutant R217Q, pH not specified in the publication, temperature not specified in the publication
190
Pyridine N-oxide
-
mutant G190D, pH not specified in the publication, temperature not specified in the publication
190
Pyridine N-oxide
-
mutant M147I, pH not specified in the publication, temperature not specified in the publication
200
Pyridine N-oxide
-
wild-type, pH not specified in the publication, temperature not specified in the publication
243
Pyridine N-oxide
-
pH 7.0, 30°C
260
Pyridine N-oxide
-
mutant G190V, pH not specified in the publication, temperature not specified in the publication
940
Pyridine N-oxide
-
mutant A181T, pH not specified in the publication, temperature not specified in the publication
14
reduced benzyl viologen
-
mutant G167N, pH not specified in the publication, temperature not specified in the publication
17
reduced benzyl viologen
-
pH 8.0, 25°C
17
reduced benzyl viologen
-
mutant W357F, pH not specified in the publication, temperature not specified in the publication
19
reduced benzyl viologen
-
mutant Q179I, pH not specified in the publication, temperature not specified in the publication
23
reduced benzyl viologen
-
mutant A178Q, pH not specified in the publication, temperature not specified in the publication
24
reduced benzyl viologen
-
mutant W357Y, pH not specified in the publication, temperature not specified in the publication
27
reduced benzyl viologen
-
mutant M147I, pH not specified in the publication, temperature not specified in the publication
39
reduced benzyl viologen
-
mutant M147L, pH not specified in the publication, temperature not specified in the publication
46
reduced benzyl viologen
-
mutant W357C, pH not specified in the publication, temperature not specified in the publication
47
reduced benzyl viologen
-
mutant W191G, pH not specified in the publication, temperature not specified in the publication
55
reduced benzyl viologen
-
mutant R217Q, pH not specified in the publication, temperature not specified in the publication
60
reduced benzyl viologen
-
mutant G190D, pH not specified in the publication, temperature not specified in the publication
61
reduced benzyl viologen
-
wild-type, pH not specified in the publication, temperature not specified in the publication
68
reduced benzyl viologen
-
mutant R149C, pH not specified in the publication, temperature not specified in the publication
110
reduced benzyl viologen
-
mutant G190V, pH not specified in the publication, temperature not specified in the publication
210
reduced benzyl viologen
-
mutant A181T, pH not specified in the publication, temperature not specified in the publication
370
reduced benzyl viologen
-
mutant T148S, pH not specified in the publication, temperature not specified in the publication
1203
Trimethylamine N-oxide
-
pH 7.0, 30°C
1900
Trimethylamine N-oxide
-
mutant Y114A, pH 8.0, temperature not specified in the publication
2300
Trimethylamine N-oxide
-
wild-type, pH 8.0, temperature not specified in the publication
4300
Trimethylamine N-oxide
-
mutant Y114F, pH 8.0, temperature not specified in the publication
11.3
Trimethylamine-N-oxide
-
mutant W116F, pH not specified in the publication, temperature not specified in the publication
134.5
Trimethylamine-N-oxide
-
wild-type, pH not specified in the publication, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
7130
2-chloropyridine N-oxide
-
pH 7.0, 30°C
2690
2-methylpyridine N-oxide
-
pH 7.0, 30°C
5280
3-amidopyridine N-oxide
-
pH 7.0, 30°C
34
3-carboxypyridine N-oxide
-
pH 7.0, 30°C
2280
3-hydroxymethylpyridine N-oxide
-
pH 7.0, 30°C
135
3-hydroxypyridine N-oxide
-
pH 7.0, 30°C
2600
3-methylpyridine N-oxide
-
pH 7.0, 30°C
1450
3alpha-hydroxybenzylpyridine N-oxide
-
pH 7.0, 30°C
413
4-chloropyridine N-oxide
-
pH 7.0, 30°C
607
4-hydroxymethylpyridine N-oxide
-
pH 7.0, 30°C
52
4-methylmorpholine N-oxide
-
pH 7.0, 30°C
592
4-methylpyridine N-oxide
-
pH 7.0, 30°C
1205
4-phenylpyridine N-oxide
-
pH 7.0, 30°C
4200 - 15000
adenosine-1N-oxide
287
dimethyldodecylamine N-oxide
-
pH 7.0, 30°C
0.816 - 17500
Dimethylsulfoxide
483
DL-methyl phenyl sulfoxide
-
pH 7.0, 30°C
5.8 - 663
methionine sulfoxide
33 - 10000
Pyridine N-oxide
50 - 23300
reduced benzyl viologen
2080
tetramethylene sulfoxide
-
pH 7.0, 30°C
34 - 830
Trimethylamine N-oxide
100 - 700
Trimethylamine-N-oxide
4200
adenosine-1N-oxide
-
mutant Y114F, pH 8.0, temperature not specified in the publication
5500
adenosine-1N-oxide
-
wild-type, pH 8.0, temperature not specified in the publication
15000
adenosine-1N-oxide
-
mutant Y114A, pH 8.0, temperature not specified in the publication
0.816
Dimethylsulfoxide
-
pH 6.0, 25°C, recombinant NapA mutant C176D
170
Dimethylsulfoxide
-
mutant Y114A, pH 8.0, temperature not specified in the publication
300
Dimethylsulfoxide
-
mutant W116F, pH not specified in the publication, temperature not specified in the publication
455
Dimethylsulfoxide
-
pH 7.0, 30°C
1000
Dimethylsulfoxide
-
mutant Y114F, pH 8.0, temperature not specified in the publication
4400
Dimethylsulfoxide
-
wild-type, pH not specified in the publication, temperature not specified in the publication
7100
Dimethylsulfoxide
-
wild-type, pH 8.0, temperature not specified in the publication
17500
Dimethylsulfoxide
W-DMSOR, pH 6.0, temperature not specified in the publication
5.8
methionine sulfoxide
-
mutant Y114A, pH 8.0, temperature not specified in the publication
9.5
methionine sulfoxide
-
mutant Y114F, pH 8.0, temperature not specified in the publication
180
methionine sulfoxide
-
wild-type, pH 8.0, temperature not specified in the publication
663
methionine sulfoxide
-
pH 7.0, 30°C
33
Pyridine N-oxide
-
mutant R217Q, pH not specified in the publication, temperature not specified in the publication
810
Pyridine N-oxide
-
mutant R149C, pH not specified in the publication, temperature not specified in the publication
850
Pyridine N-oxide
-
mutant W357F, pH not specified in the publication, temperature not specified in the publication
1000
Pyridine N-oxide
-
mutant M147L, pH not specified in the publication, temperature not specified in the publication
1100
Pyridine N-oxide
-
mutant M147I, pH not specified in the publication, temperature not specified in the publication
1100
Pyridine N-oxide
-
mutant Q179I, pH not specified in the publication, temperature not specified in the publication
1100
Pyridine N-oxide
-
mutant W357C, pH not specified in the publication, temperature not specified in the publication
1200
Pyridine N-oxide
-
mutant G190D, pH not specified in the publication, temperature not specified in the publication
1200
Pyridine N-oxide
-
mutant W357Y, pH not specified in the publication, temperature not specified in the publication
1300
Pyridine N-oxide
-
mutant G167N, pH not specified in the publication, temperature not specified in the publication
2000
Pyridine N-oxide
-
wild-type, pH not specified in the publication, temperature not specified in the publication
2100
Pyridine N-oxide
-
mutant G190V, pH not specified in the publication, temperature not specified in the publication
2100
Pyridine N-oxide
-
mutant W191G, pH not specified in the publication, temperature not specified in the publication
2580
Pyridine N-oxide
-
pH 7.0, 30°C
4000
Pyridine N-oxide
-
mutant A181T, pH not specified in the publication, temperature not specified in the publication
4000
Pyridine N-oxide
-
mutant T148S, pH not specified in the publication, temperature not specified in the publication
10000
Pyridine N-oxide
-
mutant A178Q, pH not specified in the publication, temperature not specified in the publication
50
reduced benzyl viologen
-
mutant R217Q, pH not specified in the publication, temperature not specified in the publication
370
reduced benzyl viologen
-
mutant G167N, pH not specified in the publication, temperature not specified in the publication
760
reduced benzyl viologen
-
mutant W357F, pH not specified in the publication, temperature not specified in the publication
900
reduced benzyl viologen
-
mutant R149C, pH not specified in the publication, temperature not specified in the publication
960
reduced benzyl viologen
-
mutant M147L, pH not specified in the publication, temperature not specified in the publication
1000
reduced benzyl viologen
-
mutant Q179I, pH not specified in the publication, temperature not specified in the publication
1300
reduced benzyl viologen
-
mutant W357Y, pH not specified in the publication, temperature not specified in the publication
1360
reduced benzyl viologen
-
mutant M147I, pH not specified in the publication, temperature not specified in the publication
1600
reduced benzyl viologen
-
mutant G190D, pH not specified in the publication, temperature not specified in the publication
1600
reduced benzyl viologen
-
mutant W191G, pH not specified in the publication, temperature not specified in the publication
1900
reduced benzyl viologen
-
mutant W357C, pH not specified in the publication, temperature not specified in the publication
1900
reduced benzyl viologen
-
wild-type, pH not specified in the publication, temperature not specified in the publication
3300
reduced benzyl viologen
-
mutant T148S, pH not specified in the publication, temperature not specified in the publication
3400
reduced benzyl viologen
-
mutant G190V, pH not specified in the publication, temperature not specified in the publication
5500
reduced benzyl viologen
-
mutant A181T, pH not specified in the publication, temperature not specified in the publication
23300
reduced benzyl viologen
-
mutant A178Q, pH not specified in the publication, temperature not specified in the publication
34
Trimethylamine N-oxide
-
wild-type, pH 8.0, temperature not specified in the publication
49
Trimethylamine N-oxide
-
mutant Y114F, pH 8.0, temperature not specified in the publication
59
Trimethylamine N-oxide
-
pH 7.0, 30°C
830
Trimethylamine N-oxide
-
mutant Y114A, pH 8.0, temperature not specified in the publication
100
Trimethylamine-N-oxide
-
mutant W116F, pH not specified in the publication, temperature not specified in the publication
700
Trimethylamine-N-oxide
-
wild-type, pH not specified in the publication, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
evolution
dimethyl sulfoxide reductase (DMSOR) represents the canonical member of the DMSOR family of prokaryotic pyranopterin molybdenum enzymes. DMSOR family enzymes have been classified by type, with type II/III enzymes being characterized by [(PDT)2MoVIO(OSer/Asp)]- oxidized active sites that possess N- and S-oxide reductase activity. Type III Rhodobacter capsulatus DMSOR catalyzes the reduction of dimethyl sulfoxide to dimethyl sulfide (DMS) as part of the global sulfur cycle
evolution
dimethyl sulfoxide reductase (DMSOR) represents the canonical member of the DMSOR family of prokaryotic pyranopterin molybdenum enzymes. DMSOR family enzymes have been classified by type, with type II/III enzymes being characterized by [(PDT)2MoVIO(OSer/Asp)]- oxidized active sites that possess N- and S-oxide reductase activity. Type III Rhodobacter sphaeroides DMSOR catalyzes the reduction of dimethyl sulfoxide to dimethyl sulfide (DMS) as part of the global sulfur cycle
evolution
-
respiratory enzyme members of the DMSOR family such as nitrate reductase (NR, EC 1.9.6.1), dimethyl sulfoxide reductase (DMSOR, EC 1.8.5.3), trimethylamine N-oxide reductase (TMAOR, EC 1.7.2.3), and formate dehydrogenase (FDH) contribute to this broad diversity. The DMSOR family of enzymes has diverse active sites that vary in the first coordination sphere of the molybdenum center. Many enzymes in the DMSOR family use oxygen atom transfer (OAT) reactions for substrate transformation, e.g. periplasmic nitrate reductase (Nap) and respiratory nitrate reductase (Nar) reduce nitrate to nitrite, TMAOR reduces TMAO to TMA, and DMSOR reduces DMSO to dimethyl sulfide (DMS). Enzymes that catalyze the same reaction, such as Nap and Nar, have different molybdenum coordination spheres. In NapA, molybdenum is coordinated by a cysteine residue in the 5th position and an oxo or a sulfido group in the 6th
evolution
the DMSO reductases family cofactor is the bis-molybdopterin-guanine dinucleotide (Bis-MGD) and it is composed by two pyranopterin molecules (instead of one pyranopterin as in sulfite oxidases and xanthine oxidases families), which are conjugated with nucleosides: cytosine or guanosine. In this family, the Mo atom in the MoCo is coordinated by four sulfur atoms of the pyranopterins rings and by an inorganic ion that could be selenium, oxygen, or sulfur atoms. In almost all cases, another ligand that has a role in coordination comes from an amino acid side chain that can be aspartate, serine, cysteine, and selenocysteine. Depending on this amino acid, the DMSO reductases can be classified in three types: cysteine or selenocysteine for type I, an aspartate for type II, and serine residue for type III. Enzymes belonging to this family catalyze different types of reactions: oxidation/reduction, hydroxylation/hydration, and oxygen transfer reactions. Some DMSO reductases are able to recognize more than one substrate under anaerobic conditions. Phylogenetic analysis and tree of DMSO reductases, overview. Type III enzymes are grouped in two clades constituted by DMSO reductases and TMAO reductases from bacteria and archaea. Dual activity has been described in DMSO reductases, as in the case of the Escherichia coli DMSO reductase that can reduce TMAO and other. In contrast, no DMSO reductase activity has been found in biochemically characterized TMAO reductases (EC 1.7.2.3)
evolution
the DMSO reductases family cofactor is the bis-molybdopterin-guanine dinucleotide (Bis-MGD) and it is composed by two pyranopterin molecules (instead of one pyranopterin as in sulfite oxidases and xanthine oxidases families), which are conjugated with nucleosides: cytosine or guanosine. In this family, the Mo atom in the MoCo is coordinated by four sulfur atoms of the pyranopterins rings and by an inorganic ion that could be selenium, oxygen, or sulfur atoms. In almost all cases, another ligand that has a role in coordination comes from an amino acid side chain that can be aspartate, serine, cysteine, and selenocysteine. Depending on this amino acid, the DMSO reductases can be classified in three types: cysteine or selenocysteine for type I, an aspartate for type II, and serine residue for type III. Enzymes belonging to this family catalyze different types of reactions: oxidation/reduction, hydroxylation/hydration, and oxygen transfer reactions. Some DMSO reductases are able to recognize more than one substrate under anaerobic conditions. Phylogenetic analysis and tree of DMSO reductases, overview. Type III enzymes are grouped in two clades constituted by DMSO reductases and TMAO reductases from bacteria and archaea
evolution
the enzyme belongs to the dimethyl sulfoxide (DMSO) reductase family. The DMSO reductase family enzymes are the most structurally and catalytically diverse of the three pyranopterin Mo enzyme families. The DMSO reductase family enzymes are divided into three classes (Types I, II, and III) that are distinguished from each other by their active site structure and the nature of the donor ligand that is provided by the polypeptide. DMSO reductase family enzymes are quite diverse and not all of the enzymes in this family adhere to this general classification scheme. DMSO reductases are type III enzymes and a combination of EXAFS and high resolution X-ray crystallography shows that the oxidized active site possesses a distorted six-coordinate trigonal prismatic [(MPT)2MoO(OSer)]1- coordination geometry
evolution
the enzyme belongs to the dimethyl sulfoxide (DMSO) reductase family. The DMSO reductase family enzymes are the most structurally and catalytically diverse of the three pyranopterin Mo enzyme families. The DMSO reductase family enzymes are divided into three classes (Types I, II, and III) that are distinguished from each other by their active site structure and the nature of the donor ligand that is provided by the polypeptide. DMSO reductase family enzymes are quite diverse and not all of the enzymes in this family adhere to this general classification scheme. DMSO reductases are type III enzymes and a combination of EXAFS and high resolution X-ray crystallography shows that the oxidized active site possesses a distorted six-coordinate trigonal prismatic [(MPT)2MoO(OSer)]1- coordination geometry
evolution
-
type VI and type I DMSO reductases are closely evolutionarily related. But both DMSO reductase isozymes, type I and type VI, in WP3 are functionally independent despite their close evolutionary relationship. Classification and phylogenetic analysis of DMSO respiratory subsystems in Shewanella species, overview
evolution
ubiquitous in Archaea and Bacteria, mononuclear molybdoenzymes of the dimethyl sulfoxide reductase (DMSOR) family are believed to have been core components of the first anaerobic respiratory chains, and thus present at life's origins. The family, which has been defined by the presence of a mononuclear molybdopterin or tungstopterin bis(pyranopterin guanine dinucleotide) (Mo/W-bisPGD) cofactor, is named after DMSO reductases, the first members of the family to be well-characterized. Phylogenetic analysis of DMSOR family clades and members, detailed overview. The enzyme belongs to a clade of DMSOR members that include the respiratory dimethyl sulfoxide reductase (DmsA), respiratory nitrate reductase (NarG), PsrA/PhsA/SrrA, ArxA/ArrA, and TtrA/SrdA/archaeal arsenate reductase lineages that interact with the membrane quinone pool during anaerobic respiration using the canonical subunits. The association of DMSOR members with characteristic electron transfer and membrane anchor subunits arose once early in the evolution of DSMORs and co-evolved with these representatives through multiple diversification events
evolution
-
type VI and type I DMSO reductases are closely evolutionarily related. But both DMSO reductase isozymes, type I and type VI, in WP3 are functionally independent despite their close evolutionary relationship. Classification and phylogenetic analysis of DMSO respiratory subsystems in Shewanella species, overview
-
evolution
-
the DMSO reductases family cofactor is the bis-molybdopterin-guanine dinucleotide (Bis-MGD) and it is composed by two pyranopterin molecules (instead of one pyranopterin as in sulfite oxidases and xanthine oxidases families), which are conjugated with nucleosides: cytosine or guanosine. In this family, the Mo atom in the MoCo is coordinated by four sulfur atoms of the pyranopterins rings and by an inorganic ion that could be selenium, oxygen, or sulfur atoms. In almost all cases, another ligand that has a role in coordination comes from an amino acid side chain that can be aspartate, serine, cysteine, and selenocysteine. Depending on this amino acid, the DMSO reductases can be classified in three types: cysteine or selenocysteine for type I, an aspartate for type II, and serine residue for type III. Enzymes belonging to this family catalyze different types of reactions: oxidation/reduction, hydroxylation/hydration, and oxygen transfer reactions. Some DMSO reductases are able to recognize more than one substrate under anaerobic conditions. Phylogenetic analysis and tree of DMSO reductases, overview. Type III enzymes are grouped in two clades constituted by DMSO reductases and TMAO reductases from bacteria and archaea. Dual activity has been described in DMSO reductases, as in the case of the Escherichia coli DMSO reductase that can reduce TMAO and other. In contrast, no DMSO reductase activity has been found in biochemically characterized TMAO reductases (EC 1.7.2.3)
-
evolution
-
the DMSO reductases family cofactor is the bis-molybdopterin-guanine dinucleotide (Bis-MGD) and it is composed by two pyranopterin molecules (instead of one pyranopterin as in sulfite oxidases and xanthine oxidases families), which are conjugated with nucleosides: cytosine or guanosine. In this family, the Mo atom in the MoCo is coordinated by four sulfur atoms of the pyranopterins rings and by an inorganic ion that could be selenium, oxygen, or sulfur atoms. In almost all cases, another ligand that has a role in coordination comes from an amino acid side chain that can be aspartate, serine, cysteine, and selenocysteine. Depending on this amino acid, the DMSO reductases can be classified in three types: cysteine or selenocysteine for type I, an aspartate for type II, and serine residue for type III. Enzymes belonging to this family catalyze different types of reactions: oxidation/reduction, hydroxylation/hydration, and oxygen transfer reactions. Some DMSO reductases are able to recognize more than one substrate under anaerobic conditions. Phylogenetic analysis and tree of DMSO reductases, overview. Type III enzymes are grouped in two clades constituted by DMSO reductases and TMAO reductases from bacteria and archaea
-
evolution
-
the DMSO reductases family cofactor is the bis-molybdopterin-guanine dinucleotide (Bis-MGD) and it is composed by two pyranopterin molecules (instead of one pyranopterin as in sulfite oxidases and xanthine oxidases families), which are conjugated with nucleosides: cytosine or guanosine. In this family, the Mo atom in the MoCo is coordinated by four sulfur atoms of the pyranopterins rings and by an inorganic ion that could be selenium, oxygen, or sulfur atoms. In almost all cases, another ligand that has a role in coordination comes from an amino acid side chain that can be aspartate, serine, cysteine, and selenocysteine. Depending on this amino acid, the DMSO reductases can be classified in three types: cysteine or selenocysteine for type I, an aspartate for type II, and serine residue for type III. Enzymes belonging to this family catalyze different types of reactions: oxidation/reduction, hydroxylation/hydration, and oxygen transfer reactions. Some DMSO reductases are able to recognize more than one substrate under anaerobic conditions. Phylogenetic analysis and tree of DMSO reductases, overview. Type III enzymes are grouped in two clades constituted by DMSO reductases and TMAO reductases from bacteria and archaea
-
malfunction
loss of DmsABC reduces Haemophilus influenzae fitness in interactions with human bronchial epithelial cells and neutrophils. Mutant Hi2019DELTAdmsA shows an increase in biofilm formation and increased resistance to HOCl
malfunction
-
loss of DMSO-dependent growth of the DELTAdmsA1/DELTAdmsB6 and DELTAdmsA6/DELTAdmsB1 mutants, which can be rescued by introduction of dmsA1 and dmsA6, respectively. The deficiencies of DMSO-dependent growth in DELTAdmsA1/DELTAdmsB6 and DELTAdmsA6/DELTAdmsB1 mutants are attributable to the inability to form functional DMSO reductases rather than to the silencing of the expression of both dms gene clusters. In other words, functional compensation did not occur between DmsA1 and DmsA6 or between DmsB1 and DmsB6
malfunction
-
loss of DMSO-dependent growth of the DELTAdmsA1/DELTAdmsB6 and DELTAdmsA6/DELTAdmsB1 mutants, which can be rescued by introduction of dmsA1 and dmsA6, respectively. The deficiencies of DMSO-dependent growth in DELTAdmsA1/DELTAdmsB6 and DELTAdmsA6/DELTAdmsB1 mutants are attributable to the inability to form functional DMSO reductases rather than to the silencing of the expression of both dms gene clusters. In other words, functional compensation did not occur between DmsA1 and DmsA6 or between DmsB1 and DmsB6
-
malfunction
-
loss of DmsABC reduces Haemophilus influenzae fitness in interactions with human bronchial epithelial cells and neutrophils. Mutant Hi2019DELTAdmsA shows an increase in biofilm formation and increased resistance to HOCl
-
malfunction
-
loss of DmsABC reduces Haemophilus influenzae fitness in interactions with human bronchial epithelial cells and neutrophils. Mutant Hi2019DELTAdmsA shows an increase in biofilm formation and increased resistance to HOCl
-
malfunction
-
loss of DmsABC reduces Haemophilus influenzae fitness in interactions with human bronchial epithelial cells and neutrophils. Mutant Hi2019DELTAdmsA shows an increase in biofilm formation and increased resistance to HOCl
-
malfunction
-
loss of DmsABC reduces Haemophilus influenzae fitness in interactions with human bronchial epithelial cells and neutrophils. Mutant Hi2019DELTAdmsA shows an increase in biofilm formation and increased resistance to HOCl
-
metabolism
-
two functional DMSO respiratory subsystems are essential for maximum growth of strain WP3 under in situ conditions (4C/20 MPa). A core electron transport model of DMSO reduction in the deep-sea bacterium Shewanella piezotolerans strain WP3 is proposed based on genetic and physiological data, overview. The results collectively suggest that the possession of two sets of DMSO reductases with distinct subcellular localizations may be an adaptive strategy for WP3 to achieve maximum DMSO utilization in deep-sea environments. CymA serves as a preferential electron transport protein for the type I and type VI DMSO reductases, in which type VI accepts electrons from CymA in a DmsE- and DmsF-independent manner. DmsE passes electrons to DmsA1 for DMSO reduction. Type VI DMSO reductase accepts electrons from CymA in a DmsE-independent manner, while type I DMSO reductase is strongly dependent on DmsE for electron transfer. DmsF, an integral outer membrane beta-barrel protein, facilitates electron transfer by forming a pore-like structure through the outer membrane to mediate direct interaction between the extracellular DMSO reductase and DmsE
metabolism
-
two functional DMSO respiratory subsystems are essential for maximum growth of strain WP3 under in situ conditions (4C/20 MPa). A core electron transport model of DMSO reduction in the deep-sea bacterium Shewanella piezotolerans strain WP3 is proposed based on genetic and physiological data, overview. The results collectively suggest that the possession of two sets of DMSO reductases with distinct subcellular localizations may be an adaptive strategy for WP3 to achieve maximum DMSO utilization in deep-sea environments. CymA serves as a preferential electron transport protein for the type I and type VI DMSO reductases, in which type VI accepts electrons from CymA in a DmsE- and DmsF-independent manner. DmsE passes electrons to DmsA1 for DMSO reduction. Type VI DMSO reductase accepts electrons from CymA in a DmsE-independent manner, while type I DMSO reductase is strongly dependent on DmsE for electron transfer. DmsF, an integral outer membrane beta-barrel protein, facilitates electron transfer by forming a pore-like structure through the outer membrane to mediate direct interaction between the extracellular DMSO reductase and DmsE
-
physiological function
-
anaerobic growth on sulfoxides is solely due to DmsABC expression
physiological function
-
deletion mutant of catayltic subunit DmsA is attenuated in acute disease in an aerosol infection model
physiological function
-
deletion mutants lacking dimethysulfoxide reductase retain the ability to use trimethylamine N-oxide as an electron acceptor and the trimethylamine N-oxid reductase activity is unaltered
physiological function
-
more than 50% of chlorate-resistant mutants isolated are defective in the biosynthesis of the molybdenum cofactor and all of these mutants accumulate the precursor form of the enzyme. About 45% of the mutants contain the same level of molybdenum cofactor as the parent strain and exhibit normal levels of DMSO reductase and nitrate reductase activities when chlorate is absent from the medium, but the activities of these enzymes are depressed when chlorate is present. Much of the accumulated precursor form of the enzyme in a molybdenum cofactor-deficient mutant is bound to the cytoplasmic membrane and is sensitive to treatment with proteinase K from the periplasmic side of the membrane. Results suggest that the molybdenum cofactor is necessary for proteolytic processing of the precursor to the mature enzyme on the periplasmic side of the membrane, whereas binding of the precursor to the membrane and translocation across it can occur in the absence of the cofactor
physiological function
-
mutants of Escherichia coli blocked in menaquinone biosynthesis, menB, menC, and menD, are unable to grow with DMSO as an electron acceptor, even though the terminal reductase is present in these mutants. Both growth and DMSO reduction can be restored in these mutants by growth in the presence of the menaquinone intermediates, o-succinylbenzoate and 1,4-dihydroxy-2-naphthoate, depending on the metabolic block of the mutant
physiological function
bacterial DMSO reductase and trimethylamine-N-oxide reductase (TMAO reductase) are of increasing environmental importance since they catalyze the oxidation of marine osmolytes and facilitate cloud formation and albedo
physiological function
bacterial DMSO reductase and trimethylamine-N-oxide reductase (TMAO reductase) are of increasing environmental importance since they catalyze the oxidation of marine osmolytes and facilitate cloud formation and albedo
physiological function
-
dimethyl sulfoxide (DMSO) is an environmentally significant compound due to the potential role that it plays in the biogeochemical cycle of the climatically active gas dimethyl sulfide (DMS). DMSO can be produced through the transformation of DMS by both photooxidation and biooxidation routes or by direct production from marine phytoplankton. The formation of DMSO therefore leads to the removal of DMS from seawater, effectively controlling DMS flux into the atmosphere. In addition to its roles in protecting cells against photogenerated oxidants and cryogenic damage, DMSO can also be used as an alternative electron acceptor for energy conservation through microbial dissimilatory reduction, involving the enzyme DMSo redutase. DMSO acts as a substantial sink for DMS in deep oceanic waters. Both DMSO reductase isozymes, type I and type VI, in WP3 are functionally independent despite their close evolutionary relationship
physiological function
DmsABC, a putative dimethylsulfoxide (DMSO) reductase, is required for fitness of the respiratory pathogen Haemophilus influenzae (Hi) in different models of infection. DmsABC sulfoxide reductase supports virulence in non-typeable Haemophilus influenzae. A role for DmsABC in Haemophilus influenzae infection, the conditions under which DmsABC is required in this bacterium are closely linked to interactions with the host. DmsABC is required for successful NTHi lung infection in mice. Under in vitro conditions, DmsABC is not required for Haemophilus influenzae viability
physiological function
-
dimethyl sulfoxide (DMSO) is an environmentally significant compound due to the potential role that it plays in the biogeochemical cycle of the climatically active gas dimethyl sulfide (DMS). DMSO can be produced through the transformation of DMS by both photooxidation and biooxidation routes or by direct production from marine phytoplankton. The formation of DMSO therefore leads to the removal of DMS from seawater, effectively controlling DMS flux into the atmosphere. In addition to its roles in protecting cells against photogenerated oxidants and cryogenic damage, DMSO can also be used as an alternative electron acceptor for energy conservation through microbial dissimilatory reduction, involving the enzyme DMSo redutase. DMSO acts as a substantial sink for DMS in deep oceanic waters. Both DMSO reductase isozymes, type I and type VI, in WP3 are functionally independent despite their close evolutionary relationship
-
physiological function
-
DmsABC, a putative dimethylsulfoxide (DMSO) reductase, is required for fitness of the respiratory pathogen Haemophilus influenzae (Hi) in different models of infection. DmsABC sulfoxide reductase supports virulence in non-typeable Haemophilus influenzae. A role for DmsABC in Haemophilus influenzae infection, the conditions under which DmsABC is required in this bacterium are closely linked to interactions with the host. DmsABC is required for successful NTHi lung infection in mice. Under in vitro conditions, DmsABC is not required for Haemophilus influenzae viability
-
physiological function
-
deletion mutant of catayltic subunit DmsA is attenuated in acute disease in an aerosol infection model
-
physiological function
-
DmsABC, a putative dimethylsulfoxide (DMSO) reductase, is required for fitness of the respiratory pathogen Haemophilus influenzae (Hi) in different models of infection. DmsABC sulfoxide reductase supports virulence in non-typeable Haemophilus influenzae. A role for DmsABC in Haemophilus influenzae infection, the conditions under which DmsABC is required in this bacterium are closely linked to interactions with the host. DmsABC is required for successful NTHi lung infection in mice. Under in vitro conditions, DmsABC is not required for Haemophilus influenzae viability
-
physiological function
-
DmsABC, a putative dimethylsulfoxide (DMSO) reductase, is required for fitness of the respiratory pathogen Haemophilus influenzae (Hi) in different models of infection. DmsABC sulfoxide reductase supports virulence in non-typeable Haemophilus influenzae. A role for DmsABC in Haemophilus influenzae infection, the conditions under which DmsABC is required in this bacterium are closely linked to interactions with the host. DmsABC is required for successful NTHi lung infection in mice. Under in vitro conditions, DmsABC is not required for Haemophilus influenzae viability
-
physiological function
-
DmsABC, a putative dimethylsulfoxide (DMSO) reductase, is required for fitness of the respiratory pathogen Haemophilus influenzae (Hi) in different models of infection. DmsABC sulfoxide reductase supports virulence in non-typeable Haemophilus influenzae. A role for DmsABC in Haemophilus influenzae infection, the conditions under which DmsABC is required in this bacterium are closely linked to interactions with the host. DmsABC is required for successful NTHi lung infection in mice. Under in vitro conditions, DmsABC is not required for Haemophilus influenzae viability
-
additional information
structure-function analysis of DMSO reductases, overview. Comparison of oxygen atom transfer (OAT) reactivity in different families of canonical pyranopterin Mo enzymes , including the DMSO reductase family, the sulfite oxidase (SO) family, the xanthine oxidase (XO) family enzymes, and the formate dehydrogenases. The active site structures and the nature of the ligands bound to the metal center appear to be fine-tuned so that the reactions catalyzed by pyranopterin Mo enzymes are close to thermoneutral. The DMSO reductase family enzymes are the most structurally and catalytically diverse of the three pyranopterin Mo enzyme families. The oxidized active site possesses a distorted six-coordinate trigonal prismatic [(MPT)2MoO(OSer)]1- coordination geometry
additional information
structure-function analysis of DMSO reductases, overview. Comparison of oxygen atom transfer (OAT) reactivity in different families of canonical pyranopterin Mo enzymes, including the DMSO reductase family, the sulfite oxidase (SO) family, the xanthine oxidase (XO) family enzymes, and the formate dehydrogenases. The active site structures and the nature of the ligands bound to the metal center appear to be fine-tuned so that the reactions catalyzed by pyranopterin Mo enzymes are close to thermoneutral. The DMSO reductase family enzymes are the most structurally and catalytically diverse of the three pyranopterin Mo enzyme families. The oxidized active site possesses a distorted six-coordinate trigonal prismatic [(MPT)2MoO(OSer)]1- coordination geometry
additional information
the DmsABC sulfoxide reductase is encoded by a five-gene operon, dmsABCDE that is completely conserved in genomes of Haemophilus influenzae strains. The dmsABC genes encode the structural components of the enzyme, namely, the catalytic subunit DmsA, an iron-sulfur cluster-containing electron transfer subunit, DmsB, and the membrane anchor subunit, DmsC. The dmsDE genes encode two chaperones
additional information
-
the DmsABC sulfoxide reductase is encoded by a five-gene operon, dmsABCDE that is completely conserved in genomes of Haemophilus influenzae strains. The dmsABC genes encode the structural components of the enzyme, namely, the catalytic subunit DmsA, an iron-sulfur cluster-containing electron transfer subunit, DmsB, and the membrane anchor subunit, DmsC. The dmsDE genes encode two chaperones
additional information
two desoxo molybdenum(V) complexes are synthesized and characterized as models for the paramagnetic high-g split intermediate observed in the catalytic cycle of dimethyl sulfoxide reductase (DMSOR), analysis of extended X-ray absorption fine structure (EXAFS) and electron paramagnetic resonance (EPR) data. A 6-coordinate [(PDT)2Mo(OH)(OSer)]- structure (PDT = pyranopterin dithiolene) is supported for a high-g split with four S donors from two PDT ligands, a coordinated hydroxyl ligand, and a serinate O donor. This geometry orients the redox orbital toward the substrate access channel for the two-electron reduction of substrates. Detailed overview
additional information
two desoxo molybdenum(V) complexes are synthesized and characterized as models for the paramagnetic high-g split intermediate observed in the catalytic cycle of dimethyl sulfoxide reductase (DMSOR), analysis of extended X-ray absorption fine structure (EXAFS) and electron paramagnetic resonance (EPR) data. A 6-coordinate [(PDT)2Mo(OH)(OSer)]- structure (PDT = pyranopterin dithiolene) is supported for a high-g split with four S donors from two PDT ligands, a coordinated hydroxyl ligand, and a serinate O donor. This geometry orients the redox orbital toward the substrate access channel for the two-electron reduction of substrates. Detailed overview
additional information
-
the DmsABC sulfoxide reductase is encoded by a five-gene operon, dmsABCDE that is completely conserved in genomes of Haemophilus influenzae strains. The dmsABC genes encode the structural components of the enzyme, namely, the catalytic subunit DmsA, an iron-sulfur cluster-containing electron transfer subunit, DmsB, and the membrane anchor subunit, DmsC. The dmsDE genes encode two chaperones
-
additional information
-
the DmsABC sulfoxide reductase is encoded by a five-gene operon, dmsABCDE that is completely conserved in genomes of Haemophilus influenzae strains. The dmsABC genes encode the structural components of the enzyme, namely, the catalytic subunit DmsA, an iron-sulfur cluster-containing electron transfer subunit, DmsB, and the membrane anchor subunit, DmsC. The dmsDE genes encode two chaperones
-
additional information
-
the DmsABC sulfoxide reductase is encoded by a five-gene operon, dmsABCDE that is completely conserved in genomes of Haemophilus influenzae strains. The dmsABC genes encode the structural components of the enzyme, namely, the catalytic subunit DmsA, an iron-sulfur cluster-containing electron transfer subunit, DmsB, and the membrane anchor subunit, DmsC. The dmsDE genes encode two chaperones
-
additional information
-
the DmsABC sulfoxide reductase is encoded by a five-gene operon, dmsABCDE that is completely conserved in genomes of Haemophilus influenzae strains. The dmsABC genes encode the structural components of the enzyme, namely, the catalytic subunit DmsA, an iron-sulfur cluster-containing electron transfer subunit, DmsB, and the membrane anchor subunit, DmsC. The dmsDE genes encode two chaperones
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Y114A
-
mutation in direction of the active site of trimethylamine-N-oxide reduxtase. Mutation results in decreased specificity for S-oxides and an increased specificity for trimethylamine-N-oxide
Y114F
-
mutation in direction of the active site of tiomethylamine-N-oxide reduxtase. Mutation results in decreased specificity for S-oxides and an increased specificity for trimethylamine-N-oxide
A181T
-
mutation in subunit DmsA. About 300% of wild-type catalytic efficiency
C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster. The midpoint potential of FS4[3Fe-4S] is insensitive to inhibitor 2-n-heptyl-4-hydroxyquinoline N-oxide as well as to changes in pH from 5 to 7
C38S
-
the spin-spin interaction between the reduced [4Fe-4S] cluster of subunit DmsB and the Mo(V) of the molybdo bis(molybdopterin guanine dinucleotide) cofactor of subunit DmsA is significantly modified in DmsA-C38S mutant that contains a [3Fe-4S] cluster in DmsA. In ferricyanide-oxidized glycerol-inhibited DmsAC38SBC, there is no detectable interaction between the oxidized [3Fe-4S] cluster and the molybdo bis(molybdopterin guanine dinucleotide) cofactor
C59S
mutantion renders enzyme maturation sensitive to molybdenum cofactor availability. Residue C59 is a ligand to the FS0 [4Fe-4S] cluster. In the presence of trace amounts of molybdate, the C59S variant assembles normally to the cytoplasmic membrane and supports respiratory growth on DMSO, although the ground state of FS0 as determined by EPR is converted from high-spin, S = 3/2, to low-spin, S = 1/2. In the presence of the molybdenum antagonist tungstate, wild-type enzyme lacks molybdo-bis(pyranopterin guanine dinucleotide), but is translocated via the Tat translocon and assembles on the periplasmic side of the membrane as an apoenzyme. The C59S variant cannot overcome the dual insults of amino acid substitution plus lack of molybdo-bis(pyranopterin guanine dinucleotide) , leading to degradation of the DmsABC subunits
D95A
-
mutation in electron transfer subunit DmsB
D95A/C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
D95K/C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
D97A
-
mutation in electron transfer subunit DmsB
D97A/C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
DELTAN21
mutant prevents molybdo-bis(pyranopterin guanine dinucleotide) binding and results in a degenerate [3Fe-4S] clusterform being assembled
G190D
-
mutation in subunit DmsA. About 80% of wild-type catalytic efficiency
G190V
-
mutation in subunit DmsA. About 180% of wild-type catalytic efficiency
H106A
-
mutation in electron transfer subunit DmsB
H106A/C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
H106E
-
mutation in electron transfer subunit DmsB
H106E/C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
H106I/C102S 2
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
H65R
-
mutation in subunit DmsC. Mutant blocks binding of the menaquinol analogue 2-n-heptyl-4-hydroxyquinoline-N-oxide to the protein
H85F
-
mutation in electron transfer subunit DmsB
H85F/C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
H85T
-
mutation in electron transfer subunit DmsB
H85T/C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
K77A
-
mutation in electron transfer subunit DmsB
K77A/C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
M147I
-
mutation in subunit DmsA. About 65% of wild-type catalytic efficiency
M147L
-
mutation in subunit DmsA. About 50% of wild-type catalytic efficiency
P80A
-
mutation in electron transfer subunit DmsB
P80A/C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
P80D
-
mutation in electron transfer subunit DmsB
P80H
-
mutation in electron transfer subunit DmsB
R103A
-
mutation in electron transfer subunit DmsB
R103A/C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
R149C
-
mutation in subunit DmsA. About 50% of wild-type catalytic efficiency
R61K
molybdo-bis(pyranopterin guanine dinucleotide) content is 90% of wild-type, decrease in specific activity
R77S
-
DmsA-R77S mutant, the spin-spin interaction between the reduced [4Fe-4S] cluster of subunit DmsB and the Mo(V) of the molybdo bis(molybdopterin guanine dinucleotide) cofactor of subunit DmsA is eliminated
S176A/C102S
-
double mutant DmsA-S176A and DmsB-C102S, contains an engineered [3Fe-4S] cluster in DmsB, no significant paramagnetic interaction is detected between the oxidized [3Fe-4S] cluster and the Mo(V)
S81G
-
mutation in electron transfer subunit DmsB
S81H
-
mutation in electron transfer subunit DmsB
V20Y/DELTAN21/P27G
introduction of a type I Cys group, mutations eliminate both molybdo-bis(pyranopterin guanine dinucleotide) binding and detection of a FSo cluster by EPR
V20Y/DELTAN21/P27G/R61K
addtion of mutation R61K to mutant V20Y/DELTAN21/P27G partially rescues molybdo-bis(pyranopterin guanine dinucleotide) insertion
W191G
-
mutation in subunit DmsA. About 80% of wild-type catalytic efficiency
W357C
-
mutation in subunit DmsA. About 100% of wild-type catalytic efficiency
W357F
-
mutation in subunit DmsA. About 40% of wild-type catalytic efficiency
W357Y
-
mutation in subunit DmsA. About 60% of wild-type catalytic efficiency
Y104A
-
mutation in electron transfer subunit DmsB
Y104A/C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
Y104D
-
mutation in electron transfer subunit DmsB
Y104D/C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster. Mutant dramatically lower s the midpoint potential of iron-sulfur centre FS4[3Fe-4S] from 275 to 150 mV. The midpoint potential of FS4 increases in the presence of 2-n-heptyl-4-hydroxyquinoline N-oxide and decreasing pH
Y104D/H106F/C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster
Y104E
-
mutation in electron transfer subunit DmsB
Y104E/C102S
-
mutation in electron transfer subunit DmsB. Iron-sulfur centre FS4 is assembled as a [3Fe-4S] cluster. Mutant dramatically lower s the midpoint potential of iron-sulfur centre FS4[3Fe-4S] from 275 to 145 mV
W116F
-
residue W116 forms a hydrogen bond with a single oxo ligand bound to the molybdenum ion. Mutation of this residue to phenylalanine affects the UV/visible spectrum of the purified MoVI form of dimethylsulfoxide reductase resulting in the loss of the characteristic transition at 720 nm
A178Q
-
mutation in subunit DmsA. About 1200% of wild-type catalytic efficiency
A178Q
-
mutation in subunit DmsA. Mutant is functionally impairment, with abnormal anaerobic growth with dimethylsulfoxide as the sole terminal acceptor, in a recombinant strain deleted for chromosomal dmsABC
G167N
-
mutation in subunit DmsA. About 20% of wild-type catalytic efficiency
G167N
-
mutation in subunit DmsA. Mutant is functionally impairment, with abnormal anaerobic growth with dimethylsulfoxide as the sole terminal acceptor, in a recombinant strain deleted for chromosomal dmsABC
Q179I
-
mutation in subunit DmsA. About 500% of wild-type catalytic efficiency
Q179I
-
mutation in subunit DmsA. Mutant is functionally impairment, with abnormal anaerobic growth with dimethylsulfoxide as the sole terminal acceptor, in a recombinant strain deleted for chromosomal dmsABC
R217Q
-
mutation in subunit DmsA. About 2.7% of wild-type catalytic efficiency
R217Q
-
mutation in subunit DmsA. Mutant is functionally impairment, with abnormal anaerobic growth with dimethylsulfoxide as the sole terminal acceptor, in a recombinant strain deleted for chromosomal dmsABC
T148S
-
mutation in subunit DmsA. About 150% of wild-type catalytic efficiency
T148S
-
mutation in subunit DmsA. Mutant shows altered kinetic parameters for pyridine N-oxide and dimethylsulfoxide, with Km and kcat decreasing and increasing approximately fourfold,respectively
additional information
-
construction of a number of strains lacking portions of the chromosomal dmsABC operon. The mutant strains fail to grow anaerobically on glycerol minimal medium with dimethyl sulfoxide as the sole terminal oxidant but exhibit normal growth with nitrate, fumarate, and trimethylamine N-oxide. In vivo complementation of the mutant with plasmids carrying various dms genes, singly or in combination, reveal that the expression of all three subunits is essential to restore anaerobic growth. Expression of the DmsAB subunits without DmsC results in accumulation of the catalytically active dimer in the cytoplasm. The dimer is thermolabile and catalyzes the reduction of various substrates in the presence of artificial electron donors. Dimethylnaphthoquinol is oxidized only by the holoenzyme. Results suggest that the membrane-intrinsic subunit is necessary for anchoring, stability, and electron transport. The C-terminal region of DmsB appears to interact with the anchor peptide and facilitates the membrane assembly of the catalytic dimer
additional information
-
overexpression of a subunit DmsC-dystrophin-specific amino acid sequence construct is toxic to Escherichia coli cells. Toxicity may be overcome by expression in a F0F1-ATPase mutant strain. Overexpression in COS-1 or McA-RH777 cells is not toxic and protein is localized to the endoplasmic reticulum
additional information
-
molybdopterin enzyme periplasmic nitrate reductase (NapA, EC 1.9.6.1) is utilized as a vehicle to understand the substrate preference and delineate the kinetic underpinning of the differences imposed by exchanging the molybdenum ligands. The Mo-coordinating residue mutant C176D of NapA (EC 1.9.6.1), constructed by site-directed mutagenesis, is active with DMSO (and artificial cosubstrate methyl viologen), while the wild-type NapA is not. Kinetic consequences of the exchange of the endogenous ligand to molybdenum with other ligands within the cofactor of DMSO reductase family enzymes, overview. The C176D NapA variant shows attenuated nitrate reductase activity with a kcat 17times lower than the native NapA enzyme and a Km for nitrate that is 1.5times higher than the Km for nitrate reduction by the C176S NapA variant. Proposed interaction of the Asp ligand with bound DMSO compared to a Cys ligand at the active site in NapA variants
additional information
a Hi2019DELTAdmsA strain does not show any defects in anaerobic growth on chemically defined medium (CDM), and viability is also unaffected. Although Hi2019DELTAdmsA exhibits increased biofilm formation in vitro and greater resistance to hypochlorite killing compared to the isogenic wild-type strain, its survival in contact with primary human neutrophils, in infections of cultured tissue cells, or in a mouse model of lung infection is reduced compared to wild-type, Hi2019WT. The tissue cell infection model reveals a 2fold decrease in intracellular survival, while in the mouse model of lung infection Hi2019DELTAdmsA is strongly attenuated and below detection levels at 48 h post-inoculation. While Hi2019WT is recovered in approximately equal numbers from bronchoalveolar lavage fluid (BALF) and lung tissue, survival of Hi2019DELTAdmsA is reduced in lung tissue compared to BALF samples, indicating that Hi2019DELTAdmsA has reduced access to or survival in the intracellular niche
additional information
-
a Hi2019DELTAdmsA strain does not show any defects in anaerobic growth on chemically defined medium (CDM), and viability is also unaffected. Although Hi2019DELTAdmsA exhibits increased biofilm formation in vitro and greater resistance to hypochlorite killing compared to the isogenic wild-type strain, its survival in contact with primary human neutrophils, in infections of cultured tissue cells, or in a mouse model of lung infection is reduced compared to wild-type, Hi2019WT. The tissue cell infection model reveals a 2fold decrease in intracellular survival, while in the mouse model of lung infection Hi2019DELTAdmsA is strongly attenuated and below detection levels at 48 h post-inoculation. While Hi2019WT is recovered in approximately equal numbers from bronchoalveolar lavage fluid (BALF) and lung tissue, survival of Hi2019DELTAdmsA is reduced in lung tissue compared to BALF samples, indicating that Hi2019DELTAdmsA has reduced access to or survival in the intracellular niche
additional information
-
a Hi2019DELTAdmsA strain does not show any defects in anaerobic growth on chemically defined medium (CDM), and viability is also unaffected. Although Hi2019DELTAdmsA exhibits increased biofilm formation in vitro and greater resistance to hypochlorite killing compared to the isogenic wild-type strain, its survival in contact with primary human neutrophils, in infections of cultured tissue cells, or in a mouse model of lung infection is reduced compared to wild-type, Hi2019WT. The tissue cell infection model reveals a 2fold decrease in intracellular survival, while in the mouse model of lung infection Hi2019DELTAdmsA is strongly attenuated and below detection levels at 48 h post-inoculation. While Hi2019WT is recovered in approximately equal numbers from bronchoalveolar lavage fluid (BALF) and lung tissue, survival of Hi2019DELTAdmsA is reduced in lung tissue compared to BALF samples, indicating that Hi2019DELTAdmsA has reduced access to or survival in the intracellular niche
-
additional information
-
a Hi2019DELTAdmsA strain does not show any defects in anaerobic growth on chemically defined medium (CDM), and viability is also unaffected. Although Hi2019DELTAdmsA exhibits increased biofilm formation in vitro and greater resistance to hypochlorite killing compared to the isogenic wild-type strain, its survival in contact with primary human neutrophils, in infections of cultured tissue cells, or in a mouse model of lung infection is reduced compared to wild-type, Hi2019WT. The tissue cell infection model reveals a 2fold decrease in intracellular survival, while in the mouse model of lung infection Hi2019DELTAdmsA is strongly attenuated and below detection levels at 48 h post-inoculation. While Hi2019WT is recovered in approximately equal numbers from bronchoalveolar lavage fluid (BALF) and lung tissue, survival of Hi2019DELTAdmsA is reduced in lung tissue compared to BALF samples, indicating that Hi2019DELTAdmsA has reduced access to or survival in the intracellular niche
-
additional information
-
a Hi2019DELTAdmsA strain does not show any defects in anaerobic growth on chemically defined medium (CDM), and viability is also unaffected. Although Hi2019DELTAdmsA exhibits increased biofilm formation in vitro and greater resistance to hypochlorite killing compared to the isogenic wild-type strain, its survival in contact with primary human neutrophils, in infections of cultured tissue cells, or in a mouse model of lung infection is reduced compared to wild-type, Hi2019WT. The tissue cell infection model reveals a 2fold decrease in intracellular survival, while in the mouse model of lung infection Hi2019DELTAdmsA is strongly attenuated and below detection levels at 48 h post-inoculation. While Hi2019WT is recovered in approximately equal numbers from bronchoalveolar lavage fluid (BALF) and lung tissue, survival of Hi2019DELTAdmsA is reduced in lung tissue compared to BALF samples, indicating that Hi2019DELTAdmsA has reduced access to or survival in the intracellular niche
-
additional information
-
a Hi2019DELTAdmsA strain does not show any defects in anaerobic growth on chemically defined medium (CDM), and viability is also unaffected. Although Hi2019DELTAdmsA exhibits increased biofilm formation in vitro and greater resistance to hypochlorite killing compared to the isogenic wild-type strain, its survival in contact with primary human neutrophils, in infections of cultured tissue cells, or in a mouse model of lung infection is reduced compared to wild-type, Hi2019WT. The tissue cell infection model reveals a 2fold decrease in intracellular survival, while in the mouse model of lung infection Hi2019DELTAdmsA is strongly attenuated and below detection levels at 48 h post-inoculation. While Hi2019WT is recovered in approximately equal numbers from bronchoalveolar lavage fluid (BALF) and lung tissue, survival of Hi2019DELTAdmsA is reduced in lung tissue compared to BALF samples, indicating that Hi2019DELTAdmsA has reduced access to or survival in the intracellular niche
-
additional information
-
to investigate whether the subunits from these two DMSO reductases are interchangeable, two unmarked double in-frame DELTAdmsA1/DELTAdmsB6 and DELTAdmsA6/DELTAdmsB1 deletion mutants are constructed. Physiological assays demonstrate that the two double mutants lose the ability to utilize DMSO for anaerobic growth under different conditions. Moreover, transcriptional analyses reveal that deletion of the individual gene does not eliminate the expression of other genes within the same gene cluster. The loss of DMSO-dependent growth of the DELTAdmsA1/DELTAdmsB6 and DELTAdmsA6/DELTAdmsB1 mutants can be rescued by introduction of dmsA1 and dmsA6, respectively. Two complemented strains (the DELTAdmsA1/DELTAdmsB6-dmsA1-C and DELTAdmsA6/DELTAdmsB1-dmsA6-C strains [where -C refers to complementation]) are generated. The introduction of either dmsA1 into the DELTAdmsA1/DELTAdmsB6 mutant or dmsA6 into the DELTAdmsA6/DELTAdmsB1 mutant partially restores the ability of these double mutants to utilize DMSO for anaerobic growth. Growth curves of wild-type and mutant WP3 strains with DMSO as the sole electron acceptor, overview. Mutational analysis of subcellular localization of isozymes
additional information
-
to investigate whether the subunits from these two DMSO reductases are interchangeable, two unmarked double in-frame DELTAdmsA1/DELTAdmsB6 and DELTAdmsA6/DELTAdmsB1 deletion mutants are constructed. Physiological assays demonstrate that the two double mutants lose the ability to utilize DMSO for anaerobic growth under different conditions. Moreover, transcriptional analyses reveal that deletion of the individual gene does not eliminate the expression of other genes within the same gene cluster. The loss of DMSO-dependent growth of the DELTAdmsA1/DELTAdmsB6 and DELTAdmsA6/DELTAdmsB1 mutants can be rescued by introduction of dmsA1 and dmsA6, respectively. Two complemented strains (the DELTAdmsA1/DELTAdmsB6-dmsA1-C and DELTAdmsA6/DELTAdmsB1-dmsA6-C strains [where -C refers to complementation]) are generated. The introduction of either dmsA1 into the DELTAdmsA1/DELTAdmsB6 mutant or dmsA6 into the DELTAdmsA6/DELTAdmsB1 mutant partially restores the ability of these double mutants to utilize DMSO for anaerobic growth. Growth curves of wild-type and mutant WP3 strains with DMSO as the sole electron acceptor, overview. Mutational analysis of subcellular localization of isozymes
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Schneider, F.; Lowe, F.; Huber, R.; Schindelin, H.; Kisker, C.; Knablein, J.
Crystal structure of dimethyl sulfoxide reductase from Rhodobacter capsulatus at 1.88 Ang resolution
J. Mol. Biol.
263
53-69
1996
Rhodobacter capsulatus
brenda
Fischer, B.; Schmalle, H.; Dubler, E.; Viscontini, M.
Molybdenum-pterin complexes: A functional and structural model for the binding site in the enzyme dimethyl sulfoxide reductase
Adv. Exp. Med. Biol.
338
369-372
1993
synthetic construct
brenda
Hilton, J.; Rajagopalan, K.
Identification of the molybdenum cofactor of dimethyl sulfoxide reductase from Rhodobacter sphaeroides f. sp. denitrificans as bis(molybdopterin guanine dinucleotide)molybdenum
Arch. Biochem. Biophys.
325
139-143
1996
Cereibacter sphaeroides
brenda
Adams, B.; Smith, A.T.; Bailey, S.; McEwan, A.G.; Bray, R.C.
Reactions of dimethylsulfoxide reductase from Rhodobacter capsulatus with dimethyl sulfide and with dimethyl sulfoxide: complexities revealed by conventional and stopped-flow spectrophotometry
Biochemistry
38
8501-8511
1999
Rhodobacter capsulatus
brenda
Bray, R.C.; Adams, B.; Smith, A.T.; Richards, R.L.; Lowe, D.J.; Bailey, S.
Reactions of dimethylsulfoxide reductase in the presence of dimethyl sulfide and the structure of the dimethyl sulfide-modified enzyme
Biochemistry
40
9810-9820
2001
Rhodobacter capsulatus (Q52675), Rhodobacter capsulatus
brenda
Cheng, V.W.; Rothery, R.A.; Bertero, M.G.; Strynadka, N.C.; Weiner, J.H.
Investigation of the environment surrounding iron-sulfur cluster 4 of Escherichia coli dimethylsulfoxide reductase
Biochemistry
44
8068-8077
2005
Escherichia coli
brenda
Abo, M.; Tachibana, M.; Okubo, A.; Yamazaki, S.
Enantioselective deoxygenation of alkyl aryl sulfoxides by DMSO reductase from Rhodobacter sphaeroides f.s. denitrificans
Bioorg. Med. Chem.
3
109-112
1995
Cereibacter sphaeroides, Cereibacter sphaeroides f.s. denitrificans
brenda
Miguel, L.; Meganthan, R.
Electron donors and the quinone involved in dimethyl sulfoxide reduction in Escherichia coli
Curr. Microbiol.
22
109-115
1991
Escherichia coli
-
brenda
McNamara, J.; Hillier, I.; Bhachu, T.; Garner, C.
The nature and function of the catalytic centres of the DMSO reductases
Dalton Trans.
2005
3572-3579
2005
synthetic construct
-
brenda
Solomon, P.S.; Lane, I.; Hanson, G.R.; McEwan, A.G.
Characterisation of the pterin molybdenum cofactor in dimethylsulfoxide reductase of Rhodobacter capsulatus
Eur. J. Biochem.
246
200-203
1997
Rhodobacter capsulatus
brenda
Simala-Grant, J.L.; Weiner, J.H.
Modulation of the substrate specificity of Escherichia coli dimethylsulfoxide reductase
Eur. J. Biochem.
251
510-515
1998
Escherichia coli
brenda
Ridge, J.P.; Aguey-Zinsou, K.F.; Bernhardt, P.V.; Hanson, G.R.; McEwan, A.G.
The critical role of tryptophan-116 in the catalytic cycle of dimethylsulfoxide reductase from Rhodobacter capsulatus
FEBS Lett.
563
197-202
2004
Rhodobacter capsulatus
brenda
Daruwala, R.; Meganathan, R.
Dimethyl sulfoxide reductase is not required for trimethylamine N-oxide reduction in Escherichia coli
FEMS Microbiol. Lett.
83
255-259
1991
Escherichia coli
brenda
Baltes, N.; Hennig-Pauka, I.; Jacobsen, I.; Gruber, A.; Gerlach, G.
Identification of dimethyl sulfoxide reductase in Actinobacillus pleuropneumoniae and its role in infection
Infect. Immun.
71
6784-6792
2003
Actinobacillus pleuropneumoniae, Actinobacillus pleuropneumoniae serotype 7
brenda
George, G.; Doonan, C.; Rothery, R.; Boroumand, N.; Weiner, J.
X-ray absorption spectroscopic characterization of the molybdenum site of Escherichia coli dimethyl sulfoxide reductase
Inorg. Chem.
46
2-4
2007
Escherichia coli
brenda
George, G.; Nelson, K.; Harris, H.; Doonan, C.; Rajagopalan, K.
Interaction of product analogues with the active site of Rhodobacter sphaeroides dimethyl sulfoxide reductase
Inorg. Chem.
46
3097-3104
2007
Cereibacter sphaeroides
brenda
Sambasivarao, D.; Weiner, J.
Dimethyl sulfoxide reductase of Escherichia coli: An investigation of function and assembly by use of in vivo complementation
J. Bacteriol.
173
5935-5943
1991
Escherichia coli
brenda
Zhao, Z.; Weiner, J.
Interaction of 2-n-heptyl-4-hydroxyquinoline-N-oxide with dimethyl sulfoxide reductase of Escherichia coli
J. Biol. Chem.
273
20758-20763
1998
Escherichia coli
brenda
Rothery, R.A.; Trieber, C.A.; Weiner, J.H.
Interactions between the molybdenum cofactor and iron-sulfur clusters of Escherichia coli dimethylsulfoxide reductase
J. Biol. Chem.
274
13002-13009
1999
Escherichia coli
brenda
Johnson, K.; Rajagopalan, K.
An active site tyrosine influences the ability of the dimethyl sulfoxide reductase family of molybdopterin enzymes to reduce S-oxides
J. Biol. Chem.
276
13178-13185
2001
Cereibacter sphaeroides
brenda
Stewart, L.J.; Bailey, S.; Bennett, B.; Charnock, J.M.; Garner, C.D.; McAlpine, A.S.
Dimethylsulfoxide reductase: an enzyme capable of catalysis with either molybdenum or tungsten at the active site
J. Mol. Biol.
299
593-600
2000
Rhodobacter capsulatus (Q52675), Rhodobacter capsulatus
brenda
Simala-Grant, J.; Weiner, J.
Kinetic analysis and substrate specificity of Escherichia coli dimethyl sulfoxide reductase
Microbiology
142
3231-3239
1996
Escherichia coli
brenda
Hanlon, S.; Graham, D.; Hogan, P.; Holt, R.; Reeve, C.; Shaw, A.; McEwan, A.
Asymmetric reduction of racemic sulfoxides by dimethyl sulfoxide reductases from Rhodobacter capsulatus, Escherichia coli and Proteus species
Microbiology
144
2247-2253
1998
Escherichia coli, Proteus mirabilis, Rhodobacter capsulatus
brenda
Masui, H.; Fukase, Y.; Satoh, T.
Accumulation on the cytoplasmic membrane of the precursor to dimethyl sulfoxide reductase in molybdenum cofactor-deficient mutants of Rhodobacter sphaeroides f. sp. denitrificans
Plant Cell Physiol.
33
463-469
1992
Cereibacter sphaeroides
-
brenda
Turner, R.; Busaan, J.; Lee, J.; Michalak, M.; Weiner, J.
Expression and epitope tagging of the membrane anchor subunit (DmsC) of Escherichia coli dimethyl sulfoxide reductase
Protein Eng.
10
285-290
1997
Escherichia coli
brenda
Schindelin, H.; Kisker, C.; Hilton, J.; Rajagopalan, K.; Rees, D.
Crystal structure of DMSO reductase: Redox-linked changes in molybdopterin coordination
Science
272
1615-1621
1996
Cereibacter sphaeroides
brenda
Tang, H.; Rothery, R.A.; Weiner, J.H.
A variant conferring cofactor-dependent assembly of Escherichia coli dimethylsulfoxide reductase
Biochim. Biophys. Acta
1827
730-737
2013
Escherichia coli (P18775), Escherichia coli
brenda
Hernandez-Marin, E.; Ziegler, T.
A kinetic study of dimethyl sulfoxide reductase based on density functional theory
Can. J. Chem.
88
683-693
2010
Rhodobacter capsulatus (Q52675)
-
brenda
Tang, H.; Rothery, R.A.; Voss, J.E.; Weiner, J.H.
Correct assembly of iron-sulfur cluster FS0 into Escherichia coli dimethyl sulfoxide reductase (DmsABC) is a prerequisite for molybdenum cofactor insertion
J. Biol. Chem.
286
15147-15154
2011
Escherichia coli (P18775), Escherichia coli
brenda
Li, J.; Mata, R.; Ryde, U.
Large density-functional and basis-set effects for the DMSO reductase catalyzed oxo-transfer reaction
J. Chem. Theory Comput.
9
1799-1807
2013
Rhodobacter capsulatus (Q52675)
brenda
Ha, Y.; Tenderholt, A.L.; Holm, R.H.; Hedman, B.; Hodgson, K.O.; Solomon, E.I.
Sulfur K-edge X-ray absorption spectroscopy and density functional theory calculations on monooxo Mo(IV) and bisoxo Mo(VI) bis-dithiolenes insights into the mechanism of oxo transfer in sulfite oxidase and its relation to the mechanism of DMSO reductase
J. Am. Chem. Soc.
136
9094-9105
2014
Escherichia coli (P18775)
brenda
Xiong, L.; Jian, H.; Xiao, X.
Deep-sea bacterium Shewanella piezotolerans WP3 has two dimethyl sulfoxide reductases in distinct subcellular locations
Appl. Environ. Microbiol.
83
e01262-17
2017
Shewanella piezotolerans, Shewanella piezotolerans WP3
brenda
Dhouib, R.; Nasreen, M.; Othman, D.S.M.P.; Ellis, D.; Lee, S.; Essilfie, A.T.; Hansbro, P.M.; McEwan, A.G.; Kappler, U.
The DmsABC sulfoxide reductase supports virulence in non-typeable Haemophilus influenzae
Front. Microbiol.
12
686833
2021
Haemophilus influenzae (P45004), Haemophilus influenzae, Haemophilus influenzae RD (P45004), Haemophilus influenzae DSM 11121 (P45004), Haemophilus influenzae KW20 (P45004), Haemophilus influenzae ATCC 51907 (P45004)
brenda
Kc, K.; Yang, J.; Kirk, M.L.
Addressing serine lability in a paramagnetic dimethyl sulfoxie reductase catalytic intermediate
Inorg. Chem.
60
9233-9237
2021
Rhodobacter capsulatus (Q52675), Cereibacter sphaeroides (Q57366)
brenda
Miralles-Robledillo, J.M.; Torregrosa-Crespo, J.; Martinez-Espinosa, R.M.; Pire, C.
DMSO reductase family phylogenetics and applications of extremophiles
Int. J. Mol. Sci.
20
3349
2019
Escherichia coli (P18775), Halobacterium salinarum (Q9HR74), Escherichia coli K12 (P18775), Halobacterium salinarum ATCC 700922 (Q9HR74), Halobacterium salinarum JCM 11081 (Q9HR74)
brenda
Pacheco, J.; Niks, D.; Hille, R.
Kinetic and spectroscopic characterization of tungsten-substituted DMSO reductase from Rhodobacter sphaeroides
J. Biol. Inorg. Chem.
23
295-301
2018
Cereibacter sphaeroides (Q57366), Cereibacter sphaeroides
brenda
Mintmier, B.; McGarry, J.M.; Bain, D.J.; Basu, P.
Kinetic consequences of the endogenous ligand to molybdenum in the DMSO reductase family a case study with periplasmic nitrate reductase
J. Biol. Inorg. Chem.
26
13-28
2021
Escherichia coli
brenda
Kirk, M.L.; Kc, K.
Molybdenum and tungsten cofactors and the reactions they catalyze
Met. Ions Life Sci.
20
313-342
2020
Rhodobacter capsulatus (Q52675), Cereibacter sphaeroides (Q57366)
brenda
Wells, M.; Kanmanii, N.J.; Al Zadjali, A.M.; Janecka, J.E.; Basu, P.; Oremland, R.S.; Stolz, J.F.
Methane, arsenic, selenium and the origins of the DMSO reductase family
Sci. Rep.
10
10946
2020
Escherichia coli (P18775)
brenda