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Information on EC 1.2.99.7 - aldehyde dehydrogenase (FAD-independent)
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EC Tree
1.2.99.7 aldehyde dehydrogenase (FAD-independent)IUBMB Comments
Belongs to the xanthine oxidase family of enzymes. The enzyme from Desulfovibrio sp. contains a molybdenum-molybdopterin-cytosine dinucleotide (MCD) complex and two types of [2Fe-2S] cluster per monomer, but does not contain FAD.
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
dgaor, aordd, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aldehyde oxidase
-
-
-
-
aldehyde oxidoreductase
AOR
AORDd
-
-
-
-
BV-AIDH
MOP
aldehyde oxidoreductase
-
-
-
-
AOR
Oleidesulfovibrio alaskensis NCIMB 1349
-
-
-
AOR
Oleidesulfovibrio alaskensis NCIMB 13491
-
-
-
BV-AIDH
Megalodesulfovibrio gigas NCIMB 9332
-
-
-
MOP
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an aldehyde + H2O + acceptor = a carboxylate + reduced acceptor
Belongs to the xanthine oxidase family of enzymes. The enzyme from Desulfovibrio sp. contains a molybdenum-molybdopterin-cytosine dinucleotide (MCD) complex and two types of [2Fe-2S] cluster per monomer, but does not contain FAD
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
aldehyde:acceptor oxidoreductase (FAD-independent)
Belongs to the xanthine oxidase family of enzymes. The enzyme from Desulfovibrio sp. contains a molybdenum-molybdopterin-cytosine dinucleotide (MCD) complex and two types of [2Fe-2S] cluster per monomer, but does not contain FAD.
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CAS REGISTRY NUMBER
COMMENTARY
9029-07-6
cf. EC 1.2.3.1
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2,3-dihydroxybenzaldehyde + H2O + 2,6-dichlorophenol-indophenol
2,3-dihydroxybenzoate + reduced 2,6-dichlorophenol-indophenol
Megalodesulfovibrio gigas
-
-
-
?
2,5-dihydroxybenzaldehyde + H2O + 2,6-dichlorophenol-indophenol
2,5-dihydroxybenzoate + reduced 2,6-dichlorophenol-indophenol
Megalodesulfovibrio gigas
-
-
-
?
2-hydroxybenzaldehyde + H2O + phenyazine methosulfate
2-hydroxybenzylic acid + reduced phenyazine methosulfate
A0A5K7VLU0; A0A5K7VFT8
-
-
-
?
2-nitrobenzaldehyde + H2O + phenyazine methosulfate
2-nitrobenzylic acid + reduced phenyazine methosulfate
A0A5K7VLU0; A0A5K7VFT8
-
-
-
?
2-phenylacetaldehyde + H2O + 2,6-dichlorophenol-indophenol
2-phenylacetate + reduced 2,6-dichlorophenol-indophenol
Megalodesulfovibrio gigas
-
-
-
?
3-(benzyloxy)-4-oxo-4H-pyran-2-carbaldehyde + H2O + phenyazine methosulfate
3-(benzyloxy)-4-oxo-4H-pyran-2-carboxylic acid + reduced phenyazine methosulfate
A0A5K7VLU0; A0A5K7VFT8
-
-
-
?
3-hydroxybenzaldehyde + H2O + 2,6-dichlorophenol-indophenol
3-hydroxybenzoate + reduced 2,6-dichlorophenol-indophenol
Megalodesulfovibrio gigas
-
-
-
?
3-hydroxybenzaldehyde + H2O + phenyazine methosulfate
3-hydroxybenzylic acid + reduced phenyazine methosulfate
A0A5K7VLU0; A0A5K7VFT8
-
-
-
?
3-nitrobenzaldehyde + H2O + phenyazine methosulfate
3-nitrobenzylic acid + reduced phenyazine methosulfate
A0A5K7VLU0; A0A5K7VFT8
-
-
-
?
3-phenylpropanal + H2O + 2,6-dichlorophenol-indophenol
3-phenylpropanoate + reduced 2,6-dichlorophenol-indophenol
Megalodesulfovibrio gigas
-
-
-
?
3-pyridinecarboxaldehyde + H2O + 2,6-dichlorophenol-indophenol
3-pyridinecarboxylate + reduced 2,6-dichlorophenol-indophenol
Megalodesulfovibrio gigas
-
159% of activity with acetaldehyde
-
-
?
4-hydroxybenzaldehyde + H2O + phenyazine methosulfate
4-hydroxybenzylic acid + reduced phenyazine methosulfate
A0A5K7VLU0; A0A5K7VFT8
-
-
-
?
4-nitrobenzaldehyde + H2O + phenyazine methosulfate
4-nitrobenzoic acid + reduced phenyazine methosulfate
A0A5K7VLU0; A0A5K7VFT8
-
-
-
?
acetaldehyde + H2O + 2,6-dichlorophenol-indophenol
acetate + reduced 2,6-dichlorophenol-indophenol
Megalodesulfovibrio gigas
-
-
-
-
?
acetaldehyde + H2O + 2,6-dichlorophenolindophenol
acetate + reduced 2,6-dichlorophenolindophenol
Megalodesulfovibrio gigas
-
-
-
-
?
acetaldehyde + H2O + benzylviologen
acetate + reduced benzylviologen
Megalodesulfovibrio gigas
-
natural electron aceptor not yet known, the artificial electron acceptors benzylviologen, methylviologen, 2,3-bis-(2-methoxy-4-nitro-5-sulfophenyl) and 2,6-dichlorphenol-indophenol have relative activities of 100%, 19%, 5%, and 1.3%, respectively
-
-
?
acetaldehyde + H2O + electron acceptor
acetate + reduced acceptor
Megalodesulfovibrio gigas
-
-
-
-
?
benzaldehyde + 2 ferricyanide + H2O
benzoate + 2 ferrocyanide + 2 H+
Megalodesulfovibrio gigas
-
156% of activity with 2,6-dichlorophenol-indophenol
-
-
?
benzaldehyde + H2O + 2,6-dichlorophenol-indophenol
benzoate + reduced 2,6-dichlorophenol-indophenol
benzaldehyde + H2O + 2,6-dichlorophenolindophenol
benzoate + reduced 2,6-dichlorophenol-indophenol
Megalodesulfovibrio gigas
-
-
-
?
benzaldehyde + H2O + 2,6-dichlorophenolindophenol
benzoate + reduced 2,6-dichlorophenolindophenol
benzaldehyde + H2O + cytochrome c
benzoate + reduced cytochrome c
Megalodesulfovibrio gigas
-
from horse heart, 25% of activity with 2,6-dichlorophenol-indophenol
-
-
?
benzaldehyde + H2O + cytochrome c3
benzoate + reduced cytochrome c3
Megalodesulfovibrio gigas
-
from, Desulfovibrio gigas, 20% of activity with 2,6-dichlorophenol-indophenol
-
-
?
benzaldehyde + H2O + electron acceptor
benzoate + reduced electron acceptor
Megalodesulfovibrio gigas
-
-
-
-
?
benzaldehyde + H2O + methylene blue
benzoate + reduced methylene blue
Megalodesulfovibrio gigas
-
156% of activity with 2,6-dichlorophenol-indophenol
-
-
?
benzaldehyde + H2O + oxidized 2,6-dichlorophenolindophenol
benzoate + reduced 2,6-dichlorophenol-indophenol
Megalodesulfovibrio gigas
-
-
-
-
?
benzaldehyde + H2O + phenyazine methosulfate
benzylic acid + reduced phenyazine methosulfate
A0A5K7VLU0; A0A5K7VFT8
-
-
-
?
butyraldehyde + H2O + benzylviologen
butanoate + reduced benzylviologen
Megalodesulfovibrio gigas
-
93% of activity with acetaldehyde
-
-
?
cinnamaldehyde + H2O + 2,6-dichlorophenol-indophenol
cinnamate + reduced 2,6-dichlorophenol-indophenol
Megalodesulfovibrio gigas
-
-
-
?
cinnamaldehyde + H2O + phenyazine methosulfate
cinnamic acid + reduced phenyazine methosulfate
A0A5K7VLU0; A0A5K7VFT8
-
-
-
?
formaldehyde + H2O + benzylviologen
formate + reduced benzylviologen
Megalodesulfovibrio gigas
-
16% of activity with acetaldehyde
-
-
?
furfural + H2O + benzylviologen
furfurate + reduced benzylviologen
Megalodesulfovibrio gigas
-
77% of activity with acetaldehyde
-
-
?
furfuraldehyde + H2O + 2,6-dichlorophenol-indophenol
furfurate + reduced 2,6-dichlorophenol-indophenol
Megalodesulfovibrio gigas
-
27% of activity with acetaldehyde
-
-
?
glutaraldehyde + H2O + benzylviologen
glutarate + reduced benzylviologen
Megalodesulfovibrio gigas
-
20% of activity with acetaldehyde
-
-
?
glycoaldehyde + H2O + benzylviologen
glycolate + reduced benzylviologen
Megalodesulfovibrio gigas
-
23% of activity with acetaldehyde
-
-
?
hexanal + H2O + benzylviologen
hexanoate + reduced benzylviologen
Megalodesulfovibrio gigas
-
6% of activity with acetaldehyde
-
-
?
octanal + H2O + benzylviologen
octanoate + reduced benzylviologen
Megalodesulfovibrio gigas
-
93% of activity with acetaldehyde
-
-
?
p-anisaldehyde + H2O + benzylviologen
p-anisic acid + reduced benzylviologen
Megalodesulfovibrio gigas
-
5% of activity with acetaldehyde
-
-
?
pentanal + H2O + benzylviologen
pentanoate + reduced benzylviologen
Megalodesulfovibrio gigas
-
9% of activity with acetaldehyde
-
-
?
phenylacetaldehyde + H2O + benzylviologen
phenylacetate + reduced benzylviologen
Megalodesulfovibrio gigas
-
31% of activity with acetaldehyde
-
-
?
propionaldehyde + H2O + 2,6-dichlorophenol-indophenol
propionate + reduced 2,6-dichlorophenol-indophenol
Megalodesulfovibrio gigas
-
-
-
-
?
propionaldehyde + H2O + 2,6-dichlorophenolindophenol
propionate + reduced 2,6-dichlorophenolindophenol
Megalodesulfovibrio gigas
-
-
-
-
?
propionaldehyde + H2O + benzylviologen
propionate + reduced benzylviologen
Megalodesulfovibrio gigas
-
117% of activity with acetaldehyde
-
-
?
salicylaldehyde + H2O + 2,6-dichlorophenol-indophenol
salicylate + reduced 2,6-dichlorophenol-indophenol
salicylaldehyde + H2O + 2,6-dichlorophenolindophenol
salicylate + reduced 2,6-dichlorophenolindophenol
Megalodesulfovibrio gigas
-
-
-
-
?
salicylaldehyde + H2O + benzylviologen
salicylate + reduced benzylviologen
Megalodesulfovibrio gigas
-
14% of activity with acetaldehyde
-
-
?
acetaldehyde + H2O + acceptor
acetate + reduced acceptor
Megalodesulfovibrio gigas
-
aldehyde oxidoreductase does not react with O2
-
-
?
acetaldehyde + H2O + electron acceptor
acetate + reduced electron acceptor
Megalodesulfovibrio gigas
-
-
-
-
?
acetaldehyde + H2O + electron acceptor
acetate + reduced electron acceptor
Megalodesulfovibrio gigas
-
DgAOR probably reduces aldehydes to alcohols
-
-
?
aldehyde + H2O + acceptor
carboxylate + reduced acceptor
Oleidesulfovibrio alaskensis
-
-
-
-
?
aldehyde + H2O + acceptor
carboxylate + reduced acceptor
Oleidesulfovibrio alaskensis NCIMB 1349
-
-
-
-
?
aldehyde + H2O + acceptor
carboxylate + reduced acceptor
Oleidesulfovibrio alaskensis NCIMB 13491
-
-
-
-
?
benzaldehyde + H2O + 2,6-dichlorophenol-indophenol
benzoate + reduced 2,6-dichlorophenol-indophenol
Megalodesulfovibrio gigas
-
-
-
-
?
benzaldehyde + H2O + 2,6-dichlorophenol-indophenol
benzoate + reduced 2,6-dichlorophenol-indophenol
Megalodesulfovibrio gigas
-
-
-
?
benzaldehyde + H2O + 2,6-dichlorophenolindophenol
benzoate + reduced 2,6-dichlorophenolindophenol
Oleidesulfovibrio alaskensis
-
-
-
-
?
benzaldehyde + H2O + 2,6-dichlorophenolindophenol
benzoate + reduced 2,6-dichlorophenolindophenol
Oleidesulfovibrio alaskensis NCIMB 1349
-
-
-
-
?
benzaldehyde + H2O + 2,6-dichlorophenolindophenol
benzoate + reduced 2,6-dichlorophenolindophenol
Oleidesulfovibrio alaskensis NCIMB 13491
-
-
-
-
?
benzaldehyde + H2O + benzylviologen
benzoate + reduced benzylviologen
Megalodesulfovibrio gigas
-
16% of activity with acetaldehyde
-
-
?
benzaldehyde + H2O + benzylviologen
benzoate + reduced benzylviologen
Megalodesulfovibrio gigas
-
93% of activity with acetaldehyde
-
-
?
salicylaldehyde + H2O + 2,6-dichlorophenol-indophenol
salicylate + reduced 2,6-dichlorophenol-indophenol
Megalodesulfovibrio gigas
-
-
-
-
?
salicylaldehyde + H2O + 2,6-dichlorophenol-indophenol
salicylate + reduced 2,6-dichlorophenol-indophenol
Megalodesulfovibrio gigas
-
-
-
?
additional information
?
-
Megalodesulfovibrio gigas
-
the enzyme also catalyzes the nitrite reduction with nitric oxide formation in an enzyme-, aldehyde- and nitrite-concentration- dependent manner. The enzyme catalyzes the nitrite reduction to nitric oxide in the presence of an electron donor to the enzyme, substrate (aldehyde) or not (dithionite)
-
-
?
additional information
?
-
Megalodesulfovibrio gigas
no substrates: hypoxanthine, xanthine, 1-methylxanthine, 3-methylxanthine, 1,3,7-trimethylxanthine, allopurinol, oxypurinol, isoquinoline, nicotinate, formamide
-
-
?
additional information
?
-
A0A5K7VLU0; A0A5K7VFT8
additional albeit significantly less effective acdeptors are dichlorophenolindophenol, methylene blue, ferricyanide
-
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
Megalodesulfovibrio gigas
-
the enzyme also catalyzes the nitrite reduction with nitric oxide formation in an enzyme-, aldehyde- and nitrite-concentration- dependent manner. The enzyme catalyzes the nitrite reduction to nitric oxide in the presence of an electron donor to the enzyme, substrate (aldehyde) or not (dithionite)
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Fe-S center
A0A5K7VLU0; A0A5K7VFT8
the small subunits contains a [2Fe-2S]-center
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron
Molybdenum
Iron
Megalodesulfovibrio gigas
-
DgAOR contains two spectroscopically distinguishable [2Fe-2S] centers
Iron
Megalodesulfovibrio gigas
-
the cluster ligated by a ferredoxin-type motif is close to the protein surface, whereas that ligated by an unusual cysteine motif is in contact with the molybtopterin
Molybdenum
Megalodesulfovibrio gigas
-
redox center formed by a fivefold-co-ordinated Mo atom bound to two oxygen ligands, one sulfur and one molybdopterin cytosin dinucleotide
Molybdenum
Megalodesulfovibrio gigas
-
the cluster ligated by a ferredoxin-type motif is close to the protein surface, whereas that ligated by an unusual cysteine motif is in contact with the molybtopterin
Molybdenum
Megalodesulfovibrio gigas
EPR and QM/MM study. The intraenzyme electron transfer process mediated by the pyranopterin moiety is governed by a molybdenum ligand-based regulatory mechanism
Molybdenum
Oleidesulfovibrio alaskensis
-
contains molybdopterin cytosine dinucleotide cluster, 0.6 molybdenum atoms per monomer
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-phenylacetaldehyde
Megalodesulfovibrio gigas
substrate inhibition at high concentrations
3-phenylpropanal
Megalodesulfovibrio gigas
substrate inhibition at high concentrations, suicide substrate
cyanide
Megalodesulfovibrio gigas
competitive reversible inhibitor, 30.9% inhibition at 50 mM
ethylene glycol
Megalodesulfovibrio gigas
mixed-type reversible inhibitor, 21.9% inhibition at 1 mM
glycerol
Megalodesulfovibrio gigas
competitive reversible inhibitor, 52% inhibition at 1 mM
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
24
3-(benzyloxy)-4-oxo-4H-pyran-2-carbaldehyde
A0A5K7VLU0; A0A5K7VFT8
pH 6, 30°C
-
0.0097
benzaldehyde
Megalodesulfovibrio gigas
in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.12
benzaldehyde
Megalodesulfovibrio gigas
in 50 mM Tris-HCl buffer (pH 7.6), at 37°C
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Megalodesulfovibrio gigas
Oleidesulfovibrio alaskensis
A0A5K7VLU0 i.e. small subunit, A0A5K7VFT8 i.e. large subunit
A0A5K7VLU0; A0A5K7VFT8
UniProt
brenda
Show AA Sequence and Transmembrane Helices (319 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
dimer
Megalodesulfovibrio gigas NCIMB 9332
-
2 * 62000, SDS-PAGE
-
dimer
Oleidesulfovibrio alaskensis NCIMB 1349
-
2 * 96000, SDS-PAGE
-
dimer
Oleidesulfovibrio alaskensis NCIMB 13491
-
2 * 96000, SDS-PAGE
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
kinetic and X-ray crystallographic study, structures of inactive and activated enzyme. Activation/inactivation is governed by the oxidation state of the dithiolene moiety of the pyranopterin cofactor. Incubation with dithionite plus sulfide in the presence of dioxygen produces hydrogen peroxide not associated with the enzyme activation. The peroxide molecule coordinates to molybdenum in a ny2 fashion inhibiting the enzyme activity
Megalodesulfovibrio gigas
sitting drop vapor diffusion method, using 30% (v/v) 2-propanol, 0.2 M magnesium chloride, and 0.2 M HEPES buffer (pH 7.6)
Megalodesulfovibrio gigas
vapour diffusion on sitting drops using a mixture of purified protein in 10 mM Tris-HCl, pH 7.5, and a crystallization solution of 30% isopropanol as precipitant and 200 mM MgCl2 as additive in 200 mM HEPES, pH 7.6, growth of crystals at 4°C takes approx. 3 weeks, crystals diffract to 1.28 A
Megalodesulfovibrio gigas
-
vapour-diffusion using sitting drops and a reservoir containing 100 mM Hepes, pH 7.5, 200 mM MgCl2 and 30% isopropanol, droplets are prepared by mixing 0.004 ml of a 13 mg/ml protein solution in 10 mM Tris, pH 7.6 with 0.002 ml reservoir solution, single crystals are obtained within 3-6 weeks at 4°C, crystals diffract to 3.0 A
Megalodesulfovibrio gigas
-
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
exposure to air leads to inactivation
Megalodesulfovibrio gigas
-
11936
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hensgens, C.M.H.; Hagen, W.R.; Hansen, T.A.
Purification and characterization of a benzylviologen-linked tungsten-containing aldehyde oxidoreductase from Desulfovibrio gigas
J. Bacteriol.
177
6195-6200
1995
Megalodesulfovibrio gigas
brenda
Turner, N.; Barata, B.; Bray, R.C.; Deistung, J.; Le Gall, J.; Moura, J.J.G.
The molybdenum iron-sulphur protein from Desulfovibrio gigas as a form of aldehyde oxidase
Biochem. J.
243
755-761
1987
Megalodesulfovibrio gigas
brenda
Uchida, H.; Kondo, D.; Yamashita, A.; Nagaosa, Y.; Sakurai, T.; Fujii, Y.; Fujishiro, K.; Aisaka, K.; Uwajima, T.
Purification and characterization of an aldehyde oxidase from Pseudomonas sp. KY 4690
FEMS Microbiol. Lett.
229
31-36
2003
Pseudomonas sp., Pseudomonas sp. KY 469
brenda
Andrade, S.L.; Brondino, C.D.; Feio, M.J.; Moura, I.; Moura, J.J.
Aldehyde oxidoreductase activity in Desulfovibrio alaskensis NCIMB 13491. EPR assignment of the proximal [2Fe-2S] cluster to the Mo site
Eur. J. Biochem.
267
2054-2061
2000
Oleidesulfovibrio alaskensis, Oleidesulfovibrio alaskensis NCIMB 1349, Oleidesulfovibrio alaskensis NCIMB 13491
brenda
Bray, R.C.; Turner, N.A.; Le Gall, J.; Barata, B.A.S.; Moura, J.J.G.
Information from EPR spectroscopy on the iron-sulfur centers of the iron-molybdenum protein (aldehyde oxidoreductase) of Desulfovibrio gigas
Biochem. J.
280
817-820
1991
Megalodesulfovibrio gigas
brenda
Barata, B.A.; LeGall, J.; Moura, J.J.
Aldehyde oxidoreductase activity in Desulfovibrio gigas: in vitro reconstitution of an electron-transfer chain from aldehydes to the production of molecular hydrogen
Biochemistry
32
11559-11568
1993
Megalodesulfovibrio gigas
brenda
Caldeira, J.; Belle, V.; Asso, M.; Guigliarelli, B.; Moura, I.; Moura, J.J.; Bertrand, P.
Analysis of the electron paramagnetic resonance properties of the [2Fe-2S]1+ centers in molybdenum enzymes of the xanthine oxidase family: assignment of signals I and II
Biochemistry
39
2700-2707
2000
Megalodesulfovibrio gigas
brenda
Romao, M.J.; Barata, B.A.; Archer, M.; Lobeck, K.; Moura, I.; Carrondo, M.A.; LeGall, J.; Lottspeich, F.; Huber, R.; Moura, J.J.
Subunit composition, crystallization and preliminary crystallographic studies of the Desulfovibrio gigas aldehyde oxidoreductase containing molybdenum and [2Fe-2S] centers
Eur. J. Biochem.
215
729-732
1993
Megalodesulfovibrio gigas
brenda
Thoenes, U.; Flores, O.L.; Neves, a.; Devreese, B.; Van Beeumen, J.J.; Huber, R.; Romao, M.J.; LeGall, J.; Moura, J.J.G.; Roudrigues-Pousada, C.
Molecular cloning and sequence analysis of the gene of the molybdenum-containing aldehyde oxido-reductase of Desulfovibrio gigas, the deduced amino acid sequence shows similarity to xanthine dehydrogenase
Eur. J. Biochem.
220
901-910
1994
Megalodesulfovibrio gigas
brenda
Correia dos Santos, M.M.; Sousa, P.M.; Goncalves, M.L.; Romao, M.J.; Moura, I.; Moura, J.J.
Direct electrochemistry of the Desulfovibrio gigas aldehyde oxidoreductase
Eur. J. Biochem.
271
1329-1338
2004
Megalodesulfovibrio gigas
brenda
Rebelo, J.M.; Dias, J.M.; Huber, R.; Moura, J.J.; Romao, M.J.
Structure refinement of the aldehyde oxidoreductase from Desulfovibrio gigas (MOP) at 1.28 A
J. Biol. Inorg. Chem.
6
791-800
2001
Megalodesulfovibrio gigas
brenda
Huber, R.; Hof, P.; Duarte, R.O.; Moura, J.J.; Moura, I.; Liu, M.Y.; LeGall, J.; Hille, R.; Archer, M.; Romao, M.J.
A structure-based catalytic mechanism for the xanthine oxidase family of molybdenum enzymes
Proc. Natl. Acad. Sci. USA
93
8846-8851
1996
Megalodesulfovibrio gigas
brenda
Santos-Silva, T.; Ferroni, F.; Thapper, A.; Marangon, J.; Gonzalez, P.J.; Rizzi, A.C.; Moura, I.; Moura, J.J.; Romao, M.J.; Brondino, C.D.
Kinetic, structural, and EPR studies reveal that aldehyde oxidoreductase from Desulfovibrio gigas does not need a sulfido ligand for catalysis and give evidence for a direct Mo-C interaction in a biological system
J. Am. Chem. Soc.
131
7990-7998
2009
Megalodesulfovibrio gigas (Q46509)
brenda
Maia, L.B.; Moura, J.J.
Nitrite reduction by xanthine oxidase family enzymes: a new class of nitrite reductases
J. Biol. Inorg. Chem.
16
443-460
2011
Megalodesulfovibrio gigas
brenda
Correia, H.D.; Marangon, J.; Brondino, C.D.; Moura, J.J.; Romao, M.J.; Gonzalez, P.J.; Santos-Silva, T.
Aromatic aldehydes at the active site of aldehyde oxidoreductase from Desulfovibrio gigas: reactivity and molecular details of the enzyme-substrate and enzyme-product interaction
J. Biol. Inorg. Chem.
20
219-229
2015
Megalodesulfovibrio gigas (Q46509)
brenda
Gomez, M.C.; Neuman, N.I.; Dalosto, S.D.; Gonzalez, P.J.; Moura, J.J.; Rizzi, A.C.; Brondino, C.D.
Isotropic exchange interaction between Mo and the proximal FeS center in the xanthine oxidase family member aldehyde oxidoreductase from Desulfovibrio gigas on native and polyalcohol inhibited samples: an EPR and QM/MM study
J. Biol. Inorg. Chem.
20
233-242
2015
Megalodesulfovibrio gigas (Q46509)
brenda
Marangon, J.; Correia, H.D.; Brondino, C.D.; Moura, J.J.; Romao, M.J.; Gonzalez, P.J.; Santos-Silva, T.
Kinetic and structural studies of aldehyde oxidoreductase from Desulfovibrio gigas reveal a dithiolene-based chemistry for enzyme activation and inhibition by H(2)O(2)
PLoS ONE
8
e83234
2013
Megalodesulfovibrio gigas (Q46509)
brenda
Kozono, I.; Hibi, M.; Takeuchi, M.; Ogawa, J.
Purification and characterization of molybdenum-containing aldehyde dehydrogenase that oxidizes benzyl maltol derivative from Pseudomonas nitroreducens SB32154
Biosci. Biotechnol. Biochem.
84
2390-2400
2020
Pseudomonas nitroreducens (A0A5K7VLU0 and A0A5K7VFT8)
brenda
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