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.
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.
Fe(III)-nitrilotriacetate + ferricytochrome c3
Fe(II)-nitrilotriacetate + ferrocytochrome c3
ferricytochrome c3 + 2 H2
ferrocytochrome c3 + 4 H+
-
48% relative activity compared to activity with oxidized methyl viologen
-
-
?
H+ + ferrocytochrome c3
H2 + ferricytochrome c3
H+ + neutral red
H2 + oxidized neutral red
H+ + phenosafranine
H2 + oxidized phenosafranine
-
-
-
-
?
H+ + reduced methyl viologen
H2 + methyl viologen
H2 + acceptor
H+ + reduced acceptor
electrode-grown cells overexpress the hyn-1 gene for [NiFe] hydrogenase 1
-
-
?
H2 + ammonium pertechnetate
?
H2 + benzyl viologen
H+ + reduced benzyl viologen
H2 + ferredoxin
H+ + reduced ferredoxin
Megalodesulfovibrio gigas
-
requires the presence of cytochrome c3 for the reduction of ferredoxin
-
-
?
H2 + ferricytochrome c
H+ + ferrocytochrome c
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
H2 + ferricytochrome Hmc
H+ + ferrocytochrome Hmc
H2 + methyl viologen
H+ + reduced methyl viologen
Megalodesulfovibrio gigas
-
-
-
-
?
H2 + methylene blue
H+ + reduced methylene blue
H2 + methylviologen-dication
H+ + methylviologen
H2 + mutant cytochrome c K101M
?
-
-
-
-
r
H2 + mutant cytochrome c K15M
?
-
-
-
-
r
H2 + mutant cytochrome c K26M
?
-
-
-
-
r
H2 + mutant cytochrome c K57M
?
-
-
-
-
r
H2 + mutant cytochrome c K58M
?
-
-
-
-
r
H2 + mutant cytochrome c K60M
?
-
-
-
-
r
H2 + mutant cytochrome c K72M
?
-
-
-
-
r
H2 + mutant cytochrome c K94M
?
-
-
-
-
r
H2 + mutant cytochrome c K95M
?
-
-
-
-
r
H2 + mutant cytochrome c Y65A
?
-
-
-
-
r
H2 + mutant cytochrome c Y66L
?
-
-
-
-
r
H2 + mutant cytochrome c3 K101M
?
H2 + mutant cytochrome c3 K10M
?
H2 + mutant cytochrome c3 K15M
?
H2 + mutant cytochrome c3 K26M
?
-
-
-
-
r
H2 + mutant cytochrome c3 K57M
?
-
-
-
-
r
H2 + mutant cytochrome c3 K58M
?
-
-
-
-
r
H2 + mutant cytochrome c3 K60M
?
-
-
-
-
r
H2 + mutant cytochrome c3 K72M
?
-
-
-
-
r
H2 + mutant cytochrome c3 K94M
?
-
-
-
-
r
H2 + mutant cytochrome c3 K95M
?
-
-
-
-
r
H2 + mutant cytochrome c3 Y65A
?
-
-
-
-
r
H2 + mutant cytochrome c3 Y66L
?
-
-
-
-
r
H2 + oxidized acceptor
H+ + reduced acceptor
H2 + oxidized dichloroindophenol
H+ + ?
-
30% relative activity compared to activity with oxidized methyl viologen
-
-
?
H2 + oxidized methyl viologen
H+ + reduced methyl viologen
-
100% relative activity
-
-
?
H2 + potassium ferricyanide
H+ + ?
-
34% relative activity compared to activity with oxidized methyl viologen
-
-
?
H2 + rubredoxin
H+ + reduced rubredoxin
Megalodesulfovibrio gigas
-
requires the presence of cytochrome c3 for the reduction of rubredoxin
-
-
?
H2 + [Fe] hydrogenase-cytochrome c3 complex
?
H2 + [Fe] hydrogenase-cytochrome Hmc complex
?
-
-
-
-
r
H2 +[Fe] hydrogenase-cytochrome c3-cytochrome Hmc complex
?
lactate + ammonium pertechnetate
?
lactate + ferrocytochrome c3
pyruvate + ferricytochrome c3
-
-
-
-
?
pyruvate + ferrocytochrome c3
lactate + ferricytochrome c3
-
-
-
-
?
reduced methyl viologen + H+
oxidized methyl viologen + H2
additional information
?
-
Fe(III)-nitrilotriacetate + ferricytochrome c3
Fe(II)-nitrilotriacetate + ferrocytochrome c3
-
-
-
-
?
Fe(III)-nitrilotriacetate + ferricytochrome c3
Fe(II)-nitrilotriacetate + ferrocytochrome c3
-
-
-
-
?
H+ + ferrocytochrome c3
H2 + ferricytochrome c3
-
-
-
-
?
H+ + ferrocytochrome c3
H2 + ferricytochrome c3
-
-
-
-
?
H+ + neutral red
H2 + oxidized neutral red
-
-
-
-
?
H+ + neutral red
H2 + oxidized neutral red
-
-
-
-
?
H+ + reduced methyl viologen
H2 + methyl viologen
-
-
-
-
?
H+ + reduced methyl viologen
H2 + methyl viologen
-
weak activity in H2-uptake assay
-
-
r
H+ + reduced methyl viologen
H2 + methyl viologen
-
-
-
-
?
H+ + reduced methyl viologen
H2 + methyl viologen
-
-
-
-
?
H+ + reduced methyl viologen
H2 + methyl viologen
-
-
-
-
?
H2 + ammonium pertechnetate
?
-
the reaction requires the presence of c-type cytochromes
-
-
?
H2 + ammonium pertechnetate
?
-
the reaction requires the presence of c-type cytochromes
-
-
?
H2 + benzyl viologen
H+ + reduced benzyl viologen
-
-
-
r
H2 + benzyl viologen
H+ + reduced benzyl viologen
-
-
-
r
H2 + ferricytochrome c
H+ + ferrocytochrome c
-
-
-
-
r
H2 + ferricytochrome c
H+ + ferrocytochrome c
-
nonaheme cytochrome c
-
-
?
H2 + ferricytochrome c
H+ + ferrocytochrome c
-
-
-
-
r
H2 + ferricytochrome c
H+ + ferrocytochrome c
-
nonaheme cytochrome c
-
-
?
H2 + ferricytochrome c
H+ + ferrocytochrome c
-
-
-
-
?
H2 + ferricytochrome c
H+ + ferrocytochrome c
-
-
-
-
?
H2 + ferricytochrome c
H+ + ferrocytochrome c
-
-
-
-
?
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
the type I cytochrome C3 complex is more efficient than type II cytochrome c3 complex as electron acceptor from hydrogenase
-
-
?
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
isoform type I cytochrome c3 has the potential to transfer two electrons at a time. The two isoforms type I and type II cytochrome c3 are physiological partners but only single-electron transfers occur in solution
-
-
?
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
-
-
-
?
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
-
-
-
?
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
-
-
-
r
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
tetraheme cytochrome c3
-
-
?
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
cytochrome c3 receives two protons and two electrons from hydrogenase for transport to the membrane, and converting electronic energy into proton motive force
-
-
?
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
-
-
-
r
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
tetraheme cytochrome c3
-
-
?
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
-
-
-
r
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
-
-
-
?
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
-
395559, 395562, 395563, 395566, 395571, 395574, 654261, 674919, 684509, 686734, 688655, 742006 -
-
?
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
-
-
?
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
part of an electron transport chain that mediates electronic coupling between periplasmic hydrogen oxidation and cytosolic sulfate reduction
-
-
r
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
13 kDa tetraheme cytochrome c3 forms a complex with a hexadecaheme high molecular weight cytochrome c, i.e. Hmc
-
-
r
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
the positive charges of Lys60, Lys72, Lys95, and Lys101 around heme 4 are important for formation of the transient complex with [NiFe] hydrogenase in the initial stage of the cytochrome c3 reduction. Reaction with wild-type and mutant cytochrome c3
-
-
?
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
-
-
-
?
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
part of an electron transport chain that mediates electronic coupling between periplasmic hydrogen oxidation and cytosolic sulfate reduction
-
-
r
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
13 kDa tetraheme cytochrome c3 forms a complex with a hexadecaheme high molecular weight cytochrome c, i.e. Hmc
-
-
r
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
-
-
-
?
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
-
-
-
?
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
-
-
-
?
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
the positive charges of Lys60, Lys72, Lys95, and Lys101 around heme 4 are important for formation of the transient complex with [NiFe] hydrogenase in the initial stage of the cytochrome c3 reduction. Reaction with wild-type and mutant cytochrome c3
-
-
?
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
-
-
?
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
-
-
-
?
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
Megalodesulfovibrio gigas
-
-
-
-
?
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
Megalodesulfovibrio gigas
-
-
-
-
r
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
Solidesulfovibrio fructosivorans
-
-
-
-
?
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
-
-
-
?
H2 + ferricytochrome c3
H+ + ferrocytochrome c3
-
-
-
-
?
H2 + ferricytochrome Hmc
H+ + ferrocytochrome Hmc
-
13 kDa tetraheme cytochrome c3 forms a complex with a hexadecaheme high molecular weight cytochrome c, i.e. Hmc
-
-
r
H2 + ferricytochrome Hmc
H+ + ferrocytochrome Hmc
-
13 kDa tetraheme cytochrome c3 forms a complex with a hexadecaheme high molecular weight cytochrome c, i.e. Hmc
-
-
r
H2 + methylene blue
H+ + reduced methylene blue
-
the reation is dependent on the presence of b-type cytochrome HupZ
-
-
r
H2 + methylene blue
H+ + reduced methylene blue
-
the reation is dependent on the presence of b-type cytochrome HupZ
-
-
r
H2 + methylene blue
H+ + reduced methylene blue
-
-
-
-
?
H2 + methylene blue
H+ + reduced methylene blue
-
no activity in H2-evolution assay
-
-
ir
H2 + methylene blue
H+ + reduced methylene blue
-
no activity in H2-evolution assay
-
-
ir
H2 + methylviologen-dication
H+ + methylviologen
-
-
-
?
H2 + methylviologen-dication
H+ + methylviologen
-
-
-
?
H2 + mutant cytochrome c3 K101M
?
-
-
-
-
r
H2 + mutant cytochrome c3 K101M
?
-
-
-
-
r
H2 + mutant cytochrome c3 K10M
?
-
-
-
-
r
H2 + mutant cytochrome c3 K10M
?
-
-
-
-
r
H2 + mutant cytochrome c3 K15M
?
-
-
-
-
r
H2 + mutant cytochrome c3 K15M
?
-
-
-
-
r
H2 + oxidized acceptor
H+ + reduced acceptor
-
-
-
-
?
H2 + oxidized acceptor
H+ + reduced acceptor
-
-
-
-
?
H2 + [Fe] hydrogenase-cytochrome c3 complex
?
-
-
-
-
r
H2 + [Fe] hydrogenase-cytochrome c3 complex
?
-
-
-
-
r
H2 +[Fe] hydrogenase-cytochrome c3-cytochrome Hmc complex
?
-
-
-
-
r
H2 +[Fe] hydrogenase-cytochrome c3-cytochrome Hmc complex
?
-
-
-
-
r
lactate + ammonium pertechnetate
?
-
the reaction requires the presence of c-type cytochromes
-
-
?
lactate + ammonium pertechnetate
?
-
the reaction requires the presence of c-type cytochromes
-
-
?
reduced methyl viologen + H+
oxidized methyl viologen + H2
-
-
-
-
?
reduced methyl viologen + H+
oxidized methyl viologen + H2
-
-
-
-
?
additional information
?
-
-
hydrogen-dependent platinum (IV) reducing activity in the presence of hydrogenase and its physiological electron carrier, cytochrome c3
-
-
?
additional information
?
-
-
cytochrome c3 is the natural electron acceptor
-
-
?
additional information
?
-
-
enzyme catalyzes production of H2 from Na2S2O4 in presence of cytochrome c3
-
-
?
additional information
?
-
-
enzyme can catalyze H-2H exchange in absence of added electron carriers
-
-
?
additional information
?
-
-
no reduction of ferredoxin, methylene blue or hexacyanoferrate(II) by H2
-
-
?
additional information
?
-
-
cytochrome c3 is the natural electron acceptor
-
-
?
additional information
?
-
-
nonaheme cytochrome c is a competent physiological electron acceptor for the [Ni,Fe] hydrogenase
-
-
?
additional information
?
-
-
cytochrome c3 from Desulfovibrio vulgaris strain Hildenborough, enzyme forms an electron-transfer complex with cytochrome c3 for an electron shuttle between the periplasmic enzyme and the membrane-bound cytochrome c3
-
-
?
additional information
?
-
-
enzyme reduces soluble uranium(VI) with ferrocytochrome c3 as electron donor to uranium(IV) forming the insoluble mineral uraninite, this reaction is impaired in a cytochrome c3 mutant strain
-
-
?
additional information
?
-
-
the enzyme is associated to cytochrome c3, a tetraheme 13 kDa metalloprotein, analysis of electron binding, cooperativity effects, the Redox-Bohr effect, and thermodynamics of cytochrome c3
-
-
?
additional information
?
-
-
nonaheme cytochrome c is a competent physiological electron acceptor for the [Ni,Fe] hydrogenase
-
-
?
additional information
?
-
-
cytochrome c3 is the natural electron acceptor
-
-
?
additional information
?
-
-
enzyme reduces soluble uranium(VI) with ferrocytochrome c3 as electron donor to uranium(IV) forming the insoluble mineral uraninite, this reaction is impaired in a cytochrome c3 mutant strain
-
-
?
additional information
?
-
-
the enzyme catalyzes the conversion of para-H2 to normal H2 over D2O as well as the isotope exchange reaction in the H2D2O system
-
-
?
additional information
?
-
-
enzyme reduces soluble uranium(VI) with ferrocytochrome c3 as electron donor to uranium(IV) forming the insoluble mineral uraninite, this reaction is impaired in a cytochrome c3 mutant strain
-
-
?
additional information
?
-
-
the enzyme catalyzes the conversion of para-H2 to normal H2 over D2O as well as the isotope exchange reaction in the H2D2O system
-
-
?
additional information
?
-
Solidesulfovibrio fructosivorans
-
enzyme also exhibits high Tc(VII)-reducing activity
-
-
?
additional information
?
-
Solidesulfovibrio fructosivorans
-
cytochrome c3 is the natural electron acceptor
-
-
?
additional information
?
-
-
a natural electron donor is a low-potential c3 cytochrome
-
-
?
additional information
?
-
-
a natural electron donor is a low-potential c3 cytochrome
-
-
?
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.
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.
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.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Odom, J.M.; Peck, H.D.
Hydrogenase, electron-transfer proteins, and energy coupling in the sulfate-reducing bacteria Desulfovibrio
Annu. Rev. Microbiol.
38
551-592
1984
Desulfovibrio desulfuricans, Megalodesulfovibrio gigas, Desulfovibrio vulgaris, Desulfovibrio desulfuricans Norway 4, Desulfovibrio vulgaris Hildenborough
brenda
Lalla-Maharajh, W.V.; Hall, D.O.; Cammack, R.; Rao, K.K.
Purification and properties of the membrane-bound by hydrogenase from Desulfovibrio desulfuricans
Biochem. J.
209
445-454
1983
Desulfovibrio desulfuricans, Desulfovibrio desulfuricans Norway
brenda
Yagi, T.; Honya, M.; Tamiya, N.
Purification and properties of hydrogenases of different origins
Biochim. Biophys. Acta
153
699-705
1968
Desulfovibrio desulfuricans
brenda
Yagi, T.; Kimura, K.; Daidoji, H.; Sakai, F.; Tamura, S.; Inokuchi, H.
Properties of purified hydrogenase from the particulate fraction of Desulfovibrio vulgaris, Miyazaki
J. Biochem.
79
661-671
1976
Desulfovibrio vulgaris, Desulfovibrio vulgaris Miyazaki
brenda
Grande, H.J.; van Berkel-Arts, A.; Bregh, J.; van Dijk, K.; Veeger, C.
Kinetic properties of hydrogenase isolated from Desulfovibrio vulgaris (Hildenborough)
Eur. J. Biochem.
131
81-88
1983
Desulfovibrio vulgaris
brenda
Castro, M.J.M.; Cabral, J.M.S.
Kinetic studies of hydrogenase in AOT reversed micelles
Enzyme Microb. Technol.
11
6-11
1989
Megalodesulfovibrio gigas
-
brenda
Castro, M.J.M.; Cabral, J.M.S.
Stability of hydrogenase in AOT reversed micelles
Enzyme Microb. Technol.
11
668-672
1989
Megalodesulfovibrio gigas
-
brenda
Higuchi, Y.; Yasuoka, N.; Kakudo, M.; Katsube, Y.; Yagi, T.; Inokuchi, H.
Single crystals of hydrogenase from Desulfovibrio vulgaris Miyazaki F
J. Biol. Chem.
262
2823-2825
1987
Desulfovibrio vulgaris
brenda
Rieder, R.; Cammack, R.; Hall, D.O.
Purification and properties of the soluble hydrogenase from Desulfovibrio desulfuricans (strain Norway 4)
Eur. J. Biochem.
145
637-643
1984
Desulfovibrio desulfuricans, Desulfovibrio desulfuricans Norway 4
brenda
Fritz, G.; Griesshaber, D.; Seth, O.; Kroneck, P.M.
Nonaheme cytochrome c, a new physiological electron acceptor for [Ni,Fe] hydrogenase in the sulfate-reducing bacterium Desulfovibrio desulfuricans Essex: primary sequence, molecular parameters, and redox properties
Biochemistry
40
1317-1324
2001
Desulfovibrio desulfuricans, Desulfovibrio desulfuricans Essex
brenda
Gogotov, I.N.
Hydrogenase of purple bacteria: properties and regulation of synthesis
Arch. Microbiol.
140
86-90
1984
Thiocapsa roseopersicina, Thiocapsa roseopersicina Bbs
-
brenda
Adams, M.W.W.; Hall, D.O.
Solubilization and partial purification of the membrane-bound hydrogenase of Escherichia coli
Biochem. Soc. Trans.
6
1339-1341
1978
Escherichia coli
brenda
Aubert, C.; Brugna, M.; Dolla, A.; Bruschi, M.; Giudici-Orticoni, M.T.
A sequential electron transfer from hydrogenases to cytochromes in sulfate-reducing bacteria
Biochim. Biophys. Acta
1476
85-92
2000
Desulfomicrobium norvegicum, Desulfovibrio vulgaris, Desulfovibrio vulgaris Hildenborough
brenda
De Luca, G.; De Philip, P.; Dermoun, Z.; Rousset, M.; Vermegljo, A.
Reduction of technetium(VII) by Desulfovibrio fructosovorans is mediated by the nickel-iron hydrogenase
Appl. Environ. Microbiol.
67
4583-4587
2001
Solidesulfovibrio fructosivorans
brenda
Eng, L.H.; Lewin, M.B.M.; Neujahr, H.Y.
Kinetic properties of the periplasmic hydrogenase from Desulfovibrio desulfuricans NCIMB 8372 and use in photosensitized hydrogen-production
J. Chem. Technol. Biotechnol.
56
317-324
1993
Desulfovibrio desulfuricans
-
brenda
Higuchi, Y.; Yagi, T.
Liberation of hydrogen sulfide during the catalytic action of Desulfovibrio hydrogenase under the atmosphere of hydrogen
Biochem. Biophys. Res. Commun.
255
295-299
1999
Desulfovibrio vulgaris, Desulfovibrio vulgaris Miyazaki
brenda
Payne, R.B.; Gentry, D.M.; Rapp-Giles, B.J.; Casalot, L.; Wall, J.D.
Uranium reduction by Desulfovibrio desulfuricans strain G20 and a cytochrome c3 mutant
Appl. Environ. Microbiol.
68
3129-3132
2002
Desulfovibrio desulfuricans, Desulfovibrio vulgaris, Desulfovibrio vulgaris Hildenborough
brenda
Guiral, M.; Leroy, G.; Bianco, P.; Gallice, P.; Guigliarelli, B.; Bruschi, M.; Nitschke, W.; Giudici-Orticoni, M.T.
Interaction and electron transfer between the high molecular weight cytochrome and cytochrome c3 from Desulfovibrio vulgaris Hildenborough: kinetic, microcalorimetric, EPR and electrochemical studies
Biochim. Biophys. Acta
1723
45-54
2005
Desulfovibrio vulgaris, Desulfovibrio vulgaris Hildenborough
brenda
ElAntak, L.; Morelli, X.; Bornet, O.; Hatchikian, C.; Czjzek, M.; Dolla, A.; Guerlesquin, F.
The cytochrome c3-[Fe]-hydrogenase electron-transfer complex: structural model by NMR restrained docking
FEBS Lett.
548
1-4
2003
Desulfovibrio desulfuricans
brenda
Bento, I.; Matias, P.M.; Baptista, A.M.; da Costa, P.N.; van Dongen, W.M.; Saraiva, L.M.; Schneider, T.R.; Soares, C.M.; Carrondo, M.A.
Molecular basis for redox-Bohr and cooperative effects in cytochrome c3 from Desulfovibrio desulfuricans ATCC 27774: crystallographic and modeling studies of oxidized and reduced high-resolution structures at pH 7.6
Proteins
54
135-152
2004
Desulfovibrio desulfuricans
brenda
Pereira, P.M.; Teixeira, M.; Xavier, A.V.; Louro, R.O.; Pereira, I.A.
The Tmc complex from Desulfovibrio vulgaris hildenborough is involved in transmembrane electron transfer from periplasmic hydrogen oxidation
Biochemistry
45
10359-10367
2006
Desulfovibrio vulgaris, Desulfovibrio vulgaris Hildenborough
brenda
Yahata, N.; Saitoh, T.; Takayama, Y.; Ozawa, K.; Ogata, H.; Higuchi, Y.; Akutsu, H.
Redox interaction of cytochrome c3 with [NiFe] hydrogenase from Desulfovibrio vulgaris Miyazaki F
Biochemistry
45
1653-1662
2006
Desulfovibrio vulgaris, Desulfovibrio vulgaris Miyazaki F
brenda
Vignais, P.M.
H/D exchange reactions and mechanistic aspects of the hydrogenases
Coord. Chem. Rev.
249
1677-1690
2005
Desulfovibrio vulgaris, Desulfovibrio vulgaris Miyazaki
-
brenda
Valente, F.M.; Oliveira, A.S.; Gnadt, N.; Pacheco, I.; Coelho, A.V.; Xavier, A.V.; Teixeira, M.; Soares, C.M.; Pereira, I.A.
Hydrogenases in Desulfovibrio vulgaris Hildenborough: structural and physiologic characterisation of the membrane-bound [NiFeSe] hydrogenase
J. Biol. Inorg. Chem.
10
667-682
2005
Desulfovibrio vulgaris, Desulfovibrio vulgaris Hildenborough
brenda
Pieulle, L.; Morelli, X.; Gallice, P.; Lojou, E.; Barbier, P.; Czjzek, M.; Bianco, P.; Guerlesquin, F.; Hatchikian, E.C.
The type I/type II cytochrome c3 complex: an electron transfer link in the hydrogen-sulfate reduction pathway
J. Mol. Biol.
354
73-90
2005
Desulfocurvibacter africanus
brenda
Park, H.S.; Lin, S.; Voordouw, G.
Ferric iron reduction by Desulfovibrio vulgaris Hildenborough wild type and energy metabolism mutants
Antonie van Leeuwenhoek
93
79-85
2007
Desulfovibrio vulgaris, Desulfovibrio vulgaris Hildenborough
brenda
Marshall, M.J.; Plymale, A.E.; Kennedy, D.W.; Shi, L.; Wang, Z.; Reed, S.B.; Dohnalkova, A.C.; Simonson, C.J.; Liu, C.; Saffarini, D.A.; Romine, M.F.; Zachara, J.M.; Beliaev, A.S.; Fredrickson, J.K.
Hydrogenase- and outer membrane c-type cytochrome-facilitated reduction of technetium(VII) by Shewanella oneidensis MR-1
Environ. Microbiol.
10
125-136
2008
Shewanella oneidensis, Shewanella oneidensis MR-1 / ATCC 700550
brenda
Valente, F.M.; Pereira, P.M.; Venceslau, S.S.; Regalla, M.; Coelho, A.V.; Pereira, I.A.
The [NiFeSe] hydrogenase from Desulfovibrio vulgaris Hildenborough is a bacterial lipoprotein lacking a typical lipoprotein signal peptide
FEBS Lett.
581
3341-3344
2007
Desulfovibrio vulgaris, Desulfovibrio vulgaris Hildenborough
brenda
Iida, S.; Asakura, N.; Tabata, K.; Okura, I.; Kamachi, T.
Role of positive charge of lysine residue on cytochrome c3 for electrostatic interaction with hydrogenase
J. Porphyr. Phthalocyanines
11
66-73
2007
Desulfovibrio vulgaris
-
brenda
Teixeira, V.H.; Soares, C.M.; Baptista, A.M.
Proton pathways in a [NiFe]-hydrogenase: A theoretical study
Proteins
70
1010-1022
2008
Megalodesulfovibrio gigas
brenda
Maltempi de Souza, E.; de Oliveira Pedrosa, F.; Wassem, R.; Ford, C.M.; Yates, M.G.
Genes involved in Sec-independent membrane targeting of hydrogenase in Azotobacter chroococcum
Res. Microbiol.
158
272-278
2007
Azotobacter chroococcum, Azotobacter chroococcum MCD1
brenda
Rashamuse, K.; Mutambanengwe, C.; Whiteley, C.
Enzymatic recovery of platinum (IV) from industrial wastewater using a biosulphidogenic hydrogenase
Afr. J. Biotechnol.
7
1087-1095
2008
Bacteria
-
brenda
Caffrey, S.M.; Park, H.S.; Been, J.; Gordon, P.; Sensen, C.W.; Voordouw, G.
Gene expression by the sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough grown on an iron electrode under cathodic protection conditions
Appl. Environ. Microbiol.
74
2404-2413
2008
Desulfovibrio vulgaris str. Hildenborough (Q06173), Desulfovibrio vulgaris str. Hildenborough
brenda
Li, X.; Luo, Q.; Wofford, N.Q.; Keller, K.L.; McInerney, M.J.; Wall, J.D.; Krumholz, L.R.
A molybdopterin oxidoreductase is involved in H2 oxidation in Desulfovibrio desulfuricans G20
J. Bacteriol.
191
2675-2682
2009
Desulfovibrio desulfuricans, Desulfovibrio desulfuricans G20
brenda
Walker, C.B.; He, Z.; Yang, Z.K.; Ringbauer, J.A.; He, Q.; Zhou, J.; Voordouw, G.; Wall, J.D.; Arkin, A.P.; Hazen, T.C.; Stolyar, S.; Stahl, D.A.
The electron transfer system of syntrophically grown Desulfovibrio vulgaris
J. Bacteriol.
191
5793-5801
2009
Desulfovibrio vulgaris str. Hildenborough (Q06173)
brenda
Paixao, V.B.; Vis, H.; Turner, D.L.
Redox linked conformational changes in cytochrome c3 from Desulfovibrio desulfuricans ATCC 27774
Biochemistry
49
9620-9629
2010
Desulfovibrio desulfuricans
brenda
Quintas, P.O.; Oliveira, M.S.; Catarino, T.; Turner, D.L.
Electron transfer between multihaem cytochromes c3 from Desulfovibrio africanus
Biochim. Biophys. Acta
1827
502-506
2013
Desulfocurvibacter africanus
brenda
Ciaccafava, A.; Alberola, M.; Hameury, S.; Infossi, P.; Giudici-Orticoni, M.; Lojou, E.
Hydrogen bioelectrooxidation in ionic liquids: From cytochrome c 3 redox behavior to hydrogenase activity
Electrochim. Acta
56
3359-3368
2011
Desulfovibrio vulgaris, Desulfovibrio vulgaris Hildenborough
-
brenda
Topin, J.; Rousset, M.; Antonczak, S.; Golebiowski, J.
Kinetics and thermodynamics of gas diffusion in a NiFe hydrogenase
Proteins
80
677-682
2012
Solidesulfovibrio fructosivorans (P18187)
brenda
Sugimoto, Y.; Kitazumi, Y.; Shirai, O.; Nishikawa, K.; Higuchi, Y.; Yamamoto, M.; Kano, K.
Electrostatic roles in electron transfer from [NiFe] hydrogenase to cytochrome c3 from Desulfovibrio vulgaris Miyazaki F
Biochim. Biophys. Acta
1865
481-487
2017
Desulfovibrio vulgaris, Desulfovibrio vulgaris Miyazaki F
brenda
Yagi, T.; Ogo, S.; Higuchi, Y.
Catalytic cycle of cytochrome-c3 hydrogenase, a [NiFe]-enzyme, deduced from the structures of the enzyme and the enzyme mimic
Int. J. Hydrogen Energy
39
18543-18550
2014
Desulfovibrio vulgaris (P21853), Desulfovibrio vulgaris Miyazaki F (P21853)
-
brenda