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(SeO3)2- + H2 + ?
Se + H2O + ?
(TeO3)2- + H2 + ?
Te + H2O + ?
2 H+ + reduced ferredoxin
H2 + oxidized ferredoxin
2 H+ + reduced polyferredoxin
H2 + oxidized polyferredoxin
H+ + NADH
H2 + NAD+
-
-
-
-
r
H+ + reduced benzyl viologen
H2 + oxidized benzyl viologen
-
58.8% relative activity, purified enzyme
-
-
?
H+ + reduced ferredoxin
H2 + oxidized ferredoxin
H+ + reduced methyl viologen
H2 + oxidized methyl viologen
H2 + 2 oxidized ferredoxin
2 reduced ferredoxin + 2 H+
-
-
-
?
H2 + electron acceptor
H+ + reduced electron acceptor
H2 + ferredoxin + oxidized metronidazole
H+ + ferredoxin + reduced metronidazole
H2 + methyl viologen
reduced methyl viologen + H+
H2 + NAD+
H+ + NADH
-
-
-
-
r
H2 + oxidized benzyl viologen
H+ + reduced benzyl viologen
H2 + oxidized benzyl viologen
reduced benzyl viologen + H+
-
wild-type enzyme catalysed the reduction of benzylviologen at fourfold higher rates than the reduction of ferredoxin
-
-
?
H2 + oxidized CAC3527 ferredoxin
H+ + reduced CAC3527 ferredoxin
-
mutant CAC3527 ferredoxin displays an almost 8fold lower reduction potential than wild type ferredoxin
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
H2 + oxidized ferredoxin
reduced ferredoxin + 2 H+
-
-
-
-
?
H2 + oxidized ferredoxin
reduced ferredoxin + H+
H2 + oxidized ferredoxin CAC0587
H+ + reduced ferredoxin CAC0587
-
ferredoxin CAC0587 is the standard major ferredoxin
-
-
r
H2 + oxidized ferredoxin Pet F
reduced ferredoxin Pet F + H+
-
-
-
-
?
H2 + oxidized flavodoxin CAC0587
H+ + reduced flavodoxin CAC0587
-
flavodoxin CAC0587 is the standard major flavodoxin
-
-
r
H2 + oxidized methyl viologen
H+ + reduced methyl viologen
H2 + oxidized methylene blue
H+ + reduced methylene blue
H2 + oxidized spinach ferredoxin
reduced spinach ferredoxin + H+
additional information
?
-
(SeO3)2- + H2 + ?
Se + H2O + ?
-
methyl viologen and benzyl viologen as electron acceptors
-
-
?
(SeO3)2- + H2 + ?
Se + H2O + ?
-
methyl viologen and benzyl viologen as electron acceptors
-
-
?
(TeO3)2- + H2 + ?
Te + H2O + ?
-
methyl viologen as electron acceptor
-
-
?
(TeO3)2- + H2 + ?
Te + H2O + ?
-
methyl viologen as electron acceptor
-
-
?
2 H+ + reduced ferredoxin
H2 + oxidized ferredoxin
-
-
-
-
?
2 H+ + reduced ferredoxin
H2 + oxidized ferredoxin
-
the exergonic reaction is coupled to energy conservation by means of electron-transport phosphorylation
-
-
?
2 H+ + reduced polyferredoxin
H2 + oxidized polyferredoxin
-
-
-
-
?
2 H+ + reduced polyferredoxin
H2 + oxidized polyferredoxin
-
the exergonic reaction is coupled to energy conservation by means of electron-transport phosphorylation
-
-
?
2 H+ + reduced polyferredoxin
H2 + oxidized polyferredoxin
-
-
-
-
?
2 H+ + reduced polyferredoxin
H2 + oxidized polyferredoxin
-
the exergonic reaction is coupled to energy conservation by means of electron-transport phosphorylation
-
-
?
2 H+ + reduced polyferredoxin
H2 + oxidized polyferredoxin
-
-
-
-
?
2 H+ + reduced polyferredoxin
H2 + oxidized polyferredoxin
-
the exergonic reaction is coupled to energy conservation by means of electron-transport phosphorylation
-
-
?
H+ + reduced ferredoxin
H2 + oxidized ferredoxin
-
-
-
-
?
H+ + reduced ferredoxin
H2 + oxidized ferredoxin
-
-
-
-
r
H+ + reduced ferredoxin
H2 + oxidized ferredoxin
-
reaction is proposed to be coupled to energy conservation
-
-
?
H+ + reduced ferredoxin
H2 + oxidized ferredoxin
-
hydrogen production is light-dependent, since the [FeFe] hydrogenase is coupled to the photosynthetic electron transport chain via ferredoxin
-
-
?
H+ + reduced ferredoxin
H2 + oxidized ferredoxin
-
hydrogen production is light-dependent, since the [FeFe] hydrogenase is coupled to the photosynthetic electron transport chain via ferredoxin
-
-
?
H+ + reduced ferredoxin
H2 + oxidized ferredoxin
Chlorococcum submarinum
-
hydrogen production is light-dependent, since the [FeFe] hydrogenase is coupled to the photosynthetic electron transport chain via ferredoxin
-
-
?
H+ + reduced ferredoxin
H2 + oxidized ferredoxin
-
hydrogen production is light-dependent, since the [FeFe] hydrogenase is coupled to the photosynthetic electron transport chain via ferredoxin
-
-
?
H+ + reduced ferredoxin
H2 + oxidized ferredoxin
-
-
-
-
r
H+ + reduced ferredoxin
H2 + oxidized ferredoxin
-
hydrogen production is light-dependent, since the [FeFe] hydrogenase is coupled to the photosynthetic electron transport chain via ferredoxin
-
-
?
H+ + reduced ferredoxin
H2 + oxidized ferredoxin
-
hydrogen production is light-dependent, since the [FeFe] hydrogenase is coupled to the photosynthetic electron transport chain via ferredoxin
-
-
?
H+ + reduced ferredoxin
H2 + oxidized ferredoxin
-
94.3% relative activity, purified enzyme
-
-
?
H+ + reduced ferredoxin
H2 + oxidized ferredoxin
-
hydrogen production is light-dependent, since the [FeFe] hydrogenase is coupled to the photosynthetic electron transport chain via ferredoxin
-
-
?
H+ + reduced ferredoxin
H2 + oxidized ferredoxin
-
-
-
-
?
H+ + reduced ferredoxin
H2 + oxidized ferredoxin
-
the exergonic reaction is coupled to energy conservation by means of electron-transport phosphorylation
-
-
?
H+ + reduced ferredoxin
H2 + oxidized ferredoxin
-
-
-
-
?
H+ + reduced ferredoxin
H2 + oxidized ferredoxin
-
Ech hydrogenase acts as primary proton pump in a ferredoxin-dependent electron transport system. Ech hydrogenase is necessary to generate an electrochemical ion gradient when ferredoxin is the only reducing equivalent and heterodisulfide is absent
-
-
?
H+ + reduced ferredoxin
H2 + oxidized ferredoxin
-
-
-
-
?
H+ + reduced ferredoxin
H2 + oxidized ferredoxin
-
Ech hydrogenase acts as primary proton pump in a ferredoxin-dependent electron transport system. Ech hydrogenase is necessary to generate an electrochemical ion gradient when ferredoxin is the only reducing equivalent and heterodisulfide is absent
-
-
?
H+ + reduced ferredoxin
H2 + oxidized ferredoxin
-
-
-
-
?
H+ + reduced ferredoxin
H2 + oxidized ferredoxin
-
Mbh function as a redox-driven ion pump coupling the reduction of protons with electrons derived from the oxidation of a low-potential ferredoxin to the generation of a H+ motive force
-
-
?
H+ + reduced ferredoxin
H2 + oxidized ferredoxin
-
the exergonic reaction is coupled to energy conservation by means of electron-transport phosphorylation
-
-
?
H+ + reduced ferredoxin
H2 + oxidized ferredoxin
-
hydrogen production is light-dependent, since the [FeFe] hydrogenase is coupled to the photosynthetic electron transport chain via ferredoxin
-
-
?
H+ + reduced ferredoxin
H2 + oxidized ferredoxin
-
hydrogen production is light-dependent, since the [FeFe] hydrogenase is coupled to the photosynthetic electron transport chain via ferredoxin
-
-
?
H+ + reduced methyl viologen
H2 + oxidized methyl viologen
-
-
-
-
r
H+ + reduced methyl viologen
H2 + oxidized methyl viologen
-
-
-
-
?
H+ + reduced methyl viologen
H2 + oxidized methyl viologen
-
-
-
-
?
H+ + reduced methyl viologen
H2 + oxidized methyl viologen
-
-
-
-
?
H+ + reduced methyl viologen
H2 + oxidized methyl viologen
-
-
-
-
?
H+ + reduced methyl viologen
H2 + oxidized methyl viologen
-
-
-
-
r
H+ + reduced methyl viologen
H2 + oxidized methyl viologen
-
-
-
-
r
H+ + reduced methyl viologen
H2 + oxidized methyl viologen
-
100% relative activity, purified enzyme
-
-
?
H+ + reduced methyl viologen
H2 + oxidized methyl viologen
-
-
-
-
?
H2 + electron acceptor
H+ + reduced electron acceptor
-
ferricyanide as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
-
methylene blue as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
-
ferricyanide as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
-
methylene blue as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
-
methyl viologen as electron acceptor
-
-
?
H2 + electron acceptor
H+ + reduced electron acceptor
-
methyl viologen as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
-
sulfonatopropyl viologen, sodium metatungstate and sodium silicotungstate as electron acceptor
-
-
?
H2 + electron acceptor
H+ + reduced electron acceptor
-
methyl viologen as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
-
methyl viologen as electron acceptor
-
-
?
H2 + electron acceptor
H+ + reduced electron acceptor
-
sulfonatopropyl viologen, sodium metatungstate and sodium silicotungstate as electron acceptor
-
-
?
H2 + electron acceptor
H+ + reduced electron acceptor
-
-
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
-
methylene blue as electron acceptor
-
-
?
H2 + electron acceptor
H+ + reduced electron acceptor
-
methylene blue as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
-
methyl viologen as electron acceptor
-
-
?
H2 + electron acceptor
H+ + reduced electron acceptor
-
methyl viologen as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
-
FAD and FMN as electron acceptors
-
-
?
H2 + electron acceptor
H+ + reduced electron acceptor
-
FAD, FMN or riboflavin as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
-
benzyl viologen as electron acceptor
-
-
?
H2 + electron acceptor
H+ + reduced electron acceptor
-
benzyl viologen as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
-
dichlorophenol indophenol as electron acceptor
-
-
?
H2 + electron acceptor
H+ + reduced electron acceptor
-
methylene blue as electron acceptor
-
-
?
H2 + electron acceptor
H+ + reduced electron acceptor
-
methyl viologen as electron acceptor
-
-
?
H2 + electron acceptor
H+ + reduced electron acceptor
-
methylene blue as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
-
methyl viologen as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
-
FAD, FMN or riboflavin as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
-
benzyl viologen as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
-
methylene blue as electron acceptor
-
-
?
H2 + electron acceptor
H+ + reduced electron acceptor
-
methyl viologen as electron acceptor
-
-
?
H2 + electron acceptor
H+ + reduced electron acceptor
-
benzyl viologen as electron acceptor
-
-
?
H2 + electron acceptor
H+ + reduced electron acceptor
-
dichlorophenol indophenol as electron acceptor
-
-
?
H2 + electron acceptor
H+ + reduced electron acceptor
-
methylene blue as electron acceptor
-
-
?
H2 + electron acceptor
H+ + reduced electron acceptor
-
methyl viologen as electron acceptor
-
-
?
H2 + electron acceptor
H+ + reduced electron acceptor
-
FAD and FMN as electron acceptors
-
-
?
H2 + electron acceptor
H+ + reduced electron acceptor
-
dichlorophenol indophenol as electron acceptor
-
-
?
H2 + electron acceptor
H+ + reduced electron acceptor
-
methylene blue as electron acceptor
-
-
?
H2 + electron acceptor
H+ + reduced electron acceptor
-
methyl viologen as electron acceptor
-
-
?
H2 + electron acceptor
H+ + reduced electron acceptor
-
benzyl viologen as electron acceptor
-
-
?
H2 + electron acceptor
H+ + reduced electron acceptor
-
methylene blue as electron acceptor
-
-
?
H2 + electron acceptor
H+ + reduced electron acceptor
-
methyl viologen as electron acceptor
-
-
?
H2 + electron acceptor
H+ + reduced electron acceptor
-
-
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
-
methyl viologen as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
-
benzyl viologen as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
-
methyl viologen as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
-
benzyl viologen as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
-
methylene blue as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
-
cytochrome b as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
-
methyl viologen as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
-
phenosafranine as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
-
benzyl viologen as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
-
methylene blue as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
-
cytochrome b as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
-
methyl viologen as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
-
phenosafranine as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
-
benzyl viologen as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
-
methylene blue as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
-
methyl viologen as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
-
benzyl viologen as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
-
NADP+ as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
-
cytochrome b as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
-
methyl viologen as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
-
benzyl viologen as electron acceptor
-
-
r
H2 + electron acceptor
H+ + reduced electron acceptor
-
methyl viologen as electron acceptor
-
-
r
H2 + ferredoxin + oxidized metronidazole
H+ + ferredoxin + reduced metronidazole
-
-
-
-
?
H2 + ferredoxin + oxidized metronidazole
H+ + ferredoxin + reduced metronidazole
-
-
-
-
?
H2 + methyl viologen
reduced methyl viologen + H+
-
-
-
-
?
H2 + methyl viologen
reduced methyl viologen + H+
-
-
-
-
?
H2 + methyl viologen
reduced methyl viologen + H+
-
-
-
-
?
H2 + methyl viologen
reduced methyl viologen + H+
-
-
-
-
?
H2 + oxidized benzyl viologen
H+ + reduced benzyl viologen
-
-
-
-
r
H2 + oxidized benzyl viologen
H+ + reduced benzyl viologen
-
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
-
-
-
-
?
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
-
2[4Fe4S] ferredoxin
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
-
under anoxic conditions
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
-
-
-
-
?
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
-
-
-
-
?
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
-
ferredoxin links the enzyme to photosynthesis
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
-
-
-
-
?
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
-
-
-
-
?
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
-
-
-
-
?
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
-
-
-
-
?
H2 + oxidized ferredoxin
reduced ferredoxin + H+
-
-
-
-
r
H2 + oxidized ferredoxin
reduced ferredoxin + H+
-
enzyme activity is induced in the dark under anaerobic growth conditions
-
-
r
H2 + oxidized ferredoxin
reduced ferredoxin + H+
-
-
-
-
?
H2 + oxidized ferredoxin
reduced ferredoxin + H+
-
enzyme is absolutely required for the reduction of CO2 to formylmethanofuran by H2, Ech hydrogenase provides the cell with reduced ferredoxin required as electron donor
-
-
?
H2 + oxidized ferredoxin
reduced ferredoxin + H+
-
-
-
-
?
H2 + oxidized ferredoxin
reduced ferredoxin + H+
-
-
-
-
?
H2 + oxidized ferredoxin
reduced ferredoxin + H+
-
-
-
-
?
H2 + oxidized ferredoxin
reduced ferredoxin + H+
-
-
-
-
?
H2 + oxidized ferredoxin
reduced ferredoxin + H+
-
-
-
-
?
H2 + oxidized methyl viologen
H+ + reduced methyl viologen
-
-
-
-
r
H2 + oxidized methyl viologen
H+ + reduced methyl viologen
-
-
-
-
r
H2 + oxidized methyl viologen
H+ + reduced methyl viologen
-
-
-
-
r
H2 + oxidized methyl viologen
H+ + reduced methyl viologen
-
-
-
-
r
H2 + oxidized methyl viologen
H+ + reduced methyl viologen
-
-
-
-
r
H2 + oxidized methyl viologen
H+ + reduced methyl viologen
-
-
-
-
r
H2 + oxidized methyl viologen
H+ + reduced methyl viologen
-
-
-
-
?
H2 + oxidized methyl viologen
H+ + reduced methyl viologen
-
-
-
-
r
H2 + oxidized methyl viologen
H+ + reduced methyl viologen
-
-
-
-
?
H2 + oxidized methyl viologen
H+ + reduced methyl viologen
-
-
-
-
?
H2 + oxidized methylene blue
H+ + reduced methylene blue
-
-
-
-
r
H2 + oxidized methylene blue
H+ + reduced methylene blue
-
-
-
-
r
H2 + oxidized spinach ferredoxin
reduced spinach ferredoxin + H+
-
-
-
-
?
H2 + oxidized spinach ferredoxin
reduced spinach ferredoxin + H+
-
-
-
-
?
S + NADPH
H2S + NADP+
-
-
-
?
S + NADPH
H2S + NADP+
-
-
-
-
?
additional information
?
-
-
electrodes modified with [FeFe] hydrogenase from Desulfovibrio desulfuricans (DdHydAB) catalyse both H2 oxidation and production under conditions of direct electron transfer or mediated electron transfer within the film of polymer PV2. Reversibility in electrocatalytic films is important for energy conversion applications because it combines the advantage of high current densities at low overpotential with the possibility for robust catalysis owing to the intrinsic protecting feature of the redox matrix
-
-
-
additional information
?
-
-
no activity of the purified enzyme with methylene blue, NADH, NADPH and Na-dithionite as electron-donor
-
-
?
additional information
?
-
-
major membrane protein in acetate-grown, methanol-grown or H2/CO2-grown cells
-
-
?
additional information
?
-
-
major membrane protein in acetate-grown, methanol-grown or H2/CO2-grown cells
-
-
?
additional information
?
-
-
ferredoxin is not an efficient electron carrier for both hydrogenases
-
-
?
additional information
?
-
-
ferredoxin is not an efficient electron carrier for both hydrogenases
-
-
?
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.
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Bryant, F.O.; Adams, M.W.W.
Characterization of hydrogenase from the hyperthermophilic archaebacterium, Pyrococcus furiosus
J. Biol. Chem.
264
5070-5079
1989
Pyrococcus furiosus
brenda
Fontecilla-Camps, J.C.; Frey, M.; Garcin, E.; Hatchikian, C.; Montet, Y.; Piras, C.; Vernede, X.; Volbeda, A.
Hydrogenase: a hydrogen-metabolizing enzyme. What do the crystal structures tell us about its mode of action?
Biochimie
79
661-666
1997
Megalodesulfovibrio gigas
brenda
Ma, K.; Weiss, R.; Adams, M.W.W.
Characterization of hydrogenase II from the hyperthermophilic archaeon Pyrococcus furiosus and assessment of its role in sulfur reduction
J. Bacteriol.
182
1864-1871
2000
Pyrococcus furiosus
brenda
Meuer, J.; Bartoschek, S.; Koch, J.; Kunkel, A.; Hedderich, R.
Purification and catalytic properties of Ech hydrogenase from Methanosarcina barkeri
Eur. J. Biochem.
265
325-335
1999
Methanosarcina barkeri, Methanosarcina barkeri Fusaro / DSM 804
brenda
Florin, L.; Tsokoglou, A.; Happe, T.
A novel type of iron hydrogenase in the green alga Scenedesmus obliquus is linked to the photosynthetic electron transport chain
J. Biol. Chem.
276
6125-6132
2001
Tetradesmus obliquus
brenda
Pereira, A.S.; Tavares, P.; Moura, I.; Moura, J.J.; Huynh, B.H.
Mossbauer characterization of the iron-sulfur clusters in Desulfovibrio vulgaris hydrogenase
J. Am. Chem. Soc.
123
2771-2782
2001
Desulfovibrio vulgaris
brenda
Sapra, R.; Verhagen, M.F.; Adams, M.W.
Purification and characterization of a membrane-bound hydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus
J. Bacteriol.
182
3423-3428
2000
Pyrococcus furiosus
brenda
Ueno, Y.; Kurano, N.; Miyachi, S.
Purification and characterization of hydrogenase from the marine green alga, Chlorococcum littorale
FEBS Lett.
443
144-148
1999
Alvikia littoralis
brenda
Garcin, E.; Vernede, X.; Hatchikian, E.C.; Volbeda, A.; Frey, M.; Fontecilla-Camps, J.C.
The crystal structure of a reduced [NiFeSe] hydrogenase provides an image of the activated catalytic center
Structure
7
557-566
1999
Desulfomicrobium baculatum
brenda
Romao, C.V.; Pereira, I.A.; Xavier, A.V.; LeGall, J.; Teixeira, M.
Characterization of the [NiFe] hydrogenase from the sulfate reducer Desulfovibrio vulgaris Hildenborough
Biochem. Biophys. Res. Commun.
240
75-79
1997
Desulfovibrio vulgaris, Desulfovibrio vulgaris Hildenborough ATCC 29579
brenda
Dobrindt, U.; Blaut, M.
Purification and characterization of a membrane-bound hydrogenase from Sporomusa sphaeroides involved in energy-transducing electron transport
Arch. Microbiol.
165
141-147
1996
Sporomusa sphaeroides
brenda
Fischer, J.; Quentmeier, A.; Kostka, S.; Kraft, R.; Friedrich, C.G.
Purification and characterization of the hydrogenase from Thiobacillus ferrooxidans
Arch. Microbiol.
165
289-296
1996
Acidithiobacillus ferrooxidans, Acidithiobacillus ferrooxidans ATC 19859
brenda
Yanke, L.J.; Bryant, R.D.; Laishley, E.J.
Hydrogenase I of Clostridium pasteurianum functions as a novel selenite reductase
Anaerobe
1
61-67
1995
Clostridium pasteurianum, Clostridium pasteurianum W5
brenda
Kemner, J.M.; Zeikus, J.G.
Purification and characterization of membrane-bound hydrogenase from Methanosarcina barkeri MS
Arch. Microbiol.
161
47-54
1994
Methanosarcina barkeri, Methanosarcina barkeri MS / DSM 800
-
brenda
Ma, K.; Schicho, R.N.; Kelly, R.M.; Adams, M.W.W.
Hydrogenase of the hyperthermophile Pyrococcus furiosus is an elemental sulfur reductase or sulfhydrogenase: Evidence for a sulfur-reducing hydrogenase ancestor
Proc. Natl. Acad. Sci. USA
90
5341-5344
1993
Pyrococcus furiosus
brenda
Happe, T.; Naber, J.D.
Isolation, characterization and N-terminal amino acid sequence of hydrogenase from the green alga Chlamydomonas reinhardtii
Eur. J. Biochem.
214
475-481
1993
Chlamydomonas reinhardtii, Chlamydomonas reinhardtii 137 C(+)
brenda
George, G.N.; Prince, R.C.; Stockley, K.E.; Adams, M.W.W.
X-ray-absorption-spectroscopic evidence for a novel iron cluster in hydrogenase II from Clostridium pasteurianum [published erratum appears in Biochem J 1989 Aug 1;261(3):following 1061]
Biochem. J.
259
597-600
1989
Clostridium pasteurianum
brenda
Macor, K.A.; Czernuszewicz, R.S.; Adams, M.W.W.; Spiro, T.G.
An investigation of hydrogenase I and hydrogenase II from Clostridium pasteurianum by resonance Raman spectroscopy. Evidence for a [2Fe-2S] cluster in hydrogenase I
J. Biol. Chem.
262
9945-9947
1987
Clostridium pasteurianum
brenda
Adams, M.W.W.; Mortenson, L.E.
The physical and catalytic properties of hydrogenase II of Clostridium pasteurianum. A comparison with hydrogenase I
J. Biol. Chem.
259
7045-7055
1984
Clostridium pasteurianum, Clostridium pasteurianum W5
brenda
Adams, M.W.W.; Mortenson, L.E.
The purification of hydrogenase II (uptake hydrogenase) from the anaerobic N2-fixing bacterium Clostridium pasteurianum
Biochim. Biophys. Acta
766
51-61
1984
Clostridium pasteurianum
-
brenda
Chen, J.S.; Blanchard, D.K.
Purification and properties of the H2-oxidizing (uptake) hydrogenase of the N2-fixing anaerobe Clostridium pasteurianum W5
Biochem. Biophys. Res. Commun.
122
9-16
1984
Clostridium pasteurianum, Clostridium pasteurianum W5
brenda
Roessler, P.G.; Lien, S.
Purification of hydrogenase from Chlamydomonas reinhardtii
Plant Physiol.
75
705-709
1984
Chlamydomonas reinhardtii, Chlamydomonas reinhardtii 137 C(+)
brenda
Schneider, K.; Pinkwart, M.; Jochim, K.
Purification of hydrogenases by affinity chromatography on Procion Red-agarose
Biochem. J.
213
391-398
1983
Cupriavidus necator, Clostridium pasteurianum, Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1, Clostridium pasteurianum MR 505
brenda
Van Dijk, C.; Veeger, C.
The effects of pH and redox potential on the hydrogen production activity of the hydrogenase from Megasphaera elsdenii
Eur. J. Biochem.
114
209-219
1981
Megasphaera elsdenii
brenda
Khan, S.M.; Klibanov, A.M.; Kaplan, N.O.; Kamen, M.D.
The effect of electron carriers and other ligands on oxygen stability of clostridial hydrogenase
Biochim. Biophys. Acta
659
457-465
1981
Clostridium pasteurianum
brenda
Van Dijk, C.; Grande, H.J.; Mayhew, S.G.; Veeger, C.
Properties of the hydrogenase of Megasphaera elsdenii
Eur. J. Biochem.
107
251-261
1980
Megasphaera elsdenii
brenda
Van Dijk, C.; Mayhew, S.G.; Grande, H.J.; Veeger, C.
Purification and properties of hydrogenase from Megasphaera elsdenii
Eur. J. Biochem.
102
317-330
1979
Megasphaera elsdenii, Megasphaera elsdenii LC1
brenda
Klibanov, A.M.; Kaplan, N.O.; Kamen, M.D.
Chelating agents protect hydrogenase against oxygen inactivation
Biochim. Biophys. Acta
547
411-416
1979
Clostridium pasteurianum
brenda
Chen, J.S.; Blanchard, D.K.
Isolation and properties of a unidirectional H2-oxidizing hydrogenase from the strictly anaerobic N2-fixing bacterium Clostridium pasteurianum W5
Biochem. Biophys. Res. Commun.
84
1144-1150
1978
Clostridium pasteurianum, Clostridium pasteurianum W5
brenda
Klibanov, A.M.; Kaplan, N.O.; Kamen, M.D.
A rationale for stabilization of oxygen-labile enzymes: application to a clostridial hydrogenase
Proc. Natl. Acad. Sci. USA
75
3640-3643
1978
Clostridium pasteurianum
brenda
Erbes, D.L.; Burris, R.H.
The kinetics of methyl viologen oxidation and reduction by the hydrogenase from Clostridium pasteurianum
Biochim. Biophys. Acta
525
45-54
1978
Clostridium pasteurianum, Clostridium pasteurianum W5
brenda
Chen, J.S.; Mortenson, L.E.
Purification and properties of hydrogenase from Clostridium pasteurianum W5
Biochim. Biophys. Acta
371
283-298
1974
Clostridium pasteurianum, Clostridium pasteurianum W5
brenda
Thauer, R.K.; Kufer, B.; Zhringer, M.; Jungermann, K.
The reaction of the iron-sulfur protein hydrogenase with carbon monoxide
Eur. J. Biochem.
42
447-452
1974
Clostridium pasteurianum
brenda
Nakos, G.; Mortenson, L.E.
Structural properties of hydrogenase from Clostridium pasteurianum W5
Biochemistry
10
2442-2449
1971
Clostridium pasteurianum, Clostridium pasteurianum W5
brenda
Soboh, B.; Linder, D.; Hedderich, R.
A multisubunit membrane-bound [NiFe] hydrogenase and an NADH-dependent Fe-only hydrogenase in the fermenting bacterium Thermoanaerobacter tengcongensis
Microbiology
150
2451-2463
2004
Caldanaerobacter subterraneus subsp. tengcongensis
brenda
Hedderich, R.
Energy-converting [NiFe] hydrogenases from archaea and extremophiles: ancestors of complex I
J. Bioenerg. Biomembr.
36
65-75
2004
Methanosarcina barkeri, Pyrococcus furiosus, Caldanaerobacter subterraneus subsp. tengcongensis
brenda
Semin, B.K.; Davletshina, L.N.; Novakova, A.A.; Kiseleva, T.Y.; Lanchinskaya, V.Y.; Aleksandrov, A.Y.; Seifulina, N.; Ivanov, II; Seibert, M.; Rubin, A.B.
Accumulation of ferrous iron in Chlamydomonas reinhardtii. Influence of CO2 and anaerobic induction of the reversible hydrogenase
Plant Physiol.
131
1756-1764
2003
Chlamydomonas reinhardtii
brenda
Forzi, L.; Koch, J.; Guss, A.M.; Radosevich, C.G.; Metcalf, W.W.; Hedderich, R.
Assignment of the [4Fe-4S] clusters of Ech hydrogenase from Methanosarcina barkeri to individual subunits via the characterization of site-directed mutants
FEBS J.
272
4741-4753
2005
Methanosarcina barkeri
brenda
Hedderich, R.; Forzi, L.
Energy-converting [NiFe] hydrogenases: more than just H2 activation
J. Mol. Microbiol. Biotechnol.
10
92-104
2005
Carboxydothermus hydrogenoformans, Escherichia coli, Methanosarcina barkeri, Pyrococcus furiosus, Rhodospirillum rubrum, Caldanaerobacter subterraneus subsp. tengcongensis
brenda
Ghirardi, M.L.; Posewitz, M.C.; Maness, P.; Dubini, A.; Yu, J.; Seibert, M.
Hydrogenases and hydrogen photoproduction in oxygenic photosynthetic organisms
Annu. Rev. Plant Biol.
58
71-91
2007
Chlamydomonas reinhardtii (Q9FYU1)
brenda
Akhtar, M.K.; Jones, P.R.
Deletion of iscR stimulates recombinant clostridial Fe-Fe hydrogenase activity and H2-accumulation in Escherichia coli BL21(DE3)
Appl. Microbiol. Biotechnol.
78
853-862
2008
Clostridium acetobutylicum
brenda
Chang, C.H.; King, P.W.; Ghirardi, M.L.; Kim, K.
Atomic resolution modeling of the ferredoxin:[FeFe] hydrogenase complex from Chlamydomonas reinhardtii
Biophys. J.
93
3034-3045
2007
Chlamydomonas reinhardtii
brenda
Long, H.; Chang, C.H.; King, P.W.; Ghirardi, M.L.; Kim, K.
Brownian dynamics and molecular dynamics study of the association between hydrogenase and ferredoxin from Chlamydomonas reinhardtii
Biophys. J.
95
3753-3766
2008
Chlamydomonas reinhardtii
brenda
Guerrini, O.; Burlat, B.; Leger, C.; Guigliarelli, B.; Soucaille, P.; Girbal, L.
Characterization of two 2[4Fe4S] ferredoxins from Clostridium acetobutylicum
Curr. Microbiol.
56
261-267
2008
Clostridium acetobutylicum
brenda
Demuez, M.; Cournac, L.; Guerrini, O.; Soucaille, P.; Girbal, L.
Complete activity profile of Clostridium acetobutylicum [FeFe]-hydrogenase and kinetic parameters for endogenous redox partners
FEMS Microbiol. Lett.
275
113-121
2007
Clostridium acetobutylicum
brenda
Bhosale, S.H.; Pant, A.; Khan, M.I.
Purification and characterization of putative alkaline [Ni-Fe] hydrogenase from unicellular marine green alga, Tetraselmis kochinensis NCIM 1605
Microbiol. Res.
164
131-137
2007
Tetraselmis sp. KSN-2002, Tetraselmis sp. KSN-2002 NCIM 1605
brenda
Marques, M.; Coelho, R.; Pereira, I.A.; Matias, P.M.
Purification, crystallization and preliminary crystallographic analysis of the [NiFeSe] hydrogenase from Desulfovibrio vulgaris Hildenborough
Acta Crystallogr. Sect. F
65
920-922
2009
Desulfovibrio vulgaris
brenda
Dutta, T.; Das, A.; Das, D.
Purification and characterization of [Fe]-hydrogenase from high yielding hydrogen-producing strain, Enterobacter cloacae IIT-BT08 (MTCC 5373)
Int. J. Hydrogen Energy
34
7530-7537
2009
Enterobacter cloacae
-
brenda
Long, H.; King, P.W.; Ghirardi, M.L.; Kim, K.
Hydrogenase/ferredoxin charge-transfer complexes: effect of hydrogenase mutations on the complex association
J. Phys. Chem. A
113
4060-4067
2009
Chlamydomonas reinhardtii
brenda
Stripp, S.T.; Happe, T.
How algae produce hydrogen--news from the photosynthetic hydrogenase
Dalton Trans.
2009
9960-9969
2009
Chlamydomonas moewusii, Chlamydomonas reinhardtii, Chlorococcum submarinum, Clostridium acetobutylicum, Clostridium pasteurianum, Desulfovibrio desulfuricans, Megasphaera elsdenii, Tetradesmus obliquus, [Chlorella] fusca
brenda
Schut, G.J.; Adams, M.W.
The iron-hydrogenase of Thermotoga maritima utilizes ferredoxin and NADH synergistically: a new perspective on anaerobic hydrogen production
J. Bacteriol.
191
4451-4457
2009
Thermotoga maritima
brenda
Major, T.A.; Liu, Y.; Whitman, W.B.
Characterization of energy-conserving hydrogenase B in Methanococcus maripaludis
J. Bacteriol.
192
4022-4030
2010
Methanococcus maripaludis
brenda
Welte, C.; Kallnik, V.; Grapp, M.; Bender, G.; Ragsdale, S.; Deppenmeier, U.
Function of Ech hydrogenase in ferredoxin-dependent, membrane-bound electron transport in Methanosarcina mazei
J. Bacteriol.
192
674-678
2010
Methanosarcina mazei
brenda
Silva, P.J.; van den Ban, E.C.; Wassink, H.; Haaker, H.; de Castro, B.; Robb, F.T.; Hagen, W.R.
Enzymes of hydrogen metabolism in Pyrococcus furiosus
Eur. J. Biochem.
267
6541-6551
2000
Pyrococcus furiosus (Q8U0Z6), Pyrococcus furiosus (Q8U0Z7), Pyrococcus furiosus (Q8U0Z8), Pyrococcus furiosus
brenda
Silakov, A.; Reijerse, E.; Lubitz, W.
Unraveling the electronic properties of the photoinduced states of the H-cluster in the [FeFe] hydrogenase from D. desulfuricans
Eur. J. Inorg. Chem.
2011
1056-1066
2011
Desulfovibrio desulfuricans
-
brenda
Ghysels, B.; Godaux, D.; Matagne, R.; Cardol, P.; Franck, F.
Function of the chloroplast hydrogenase in the microalga Chlamydomonas: The role of hydrogenase and state transitions during photosynthetic activation in anaerobiosis
PLoS ONE
8
e64161
2013
Chlamydomonas reinhardtii
brenda
Welte, C.; Krtzer, C.; Deppenmeier, U.
Involvement of Ech hydrogenase in energy conservation of Methanosarcina mazei
FEBS J.
277
3396-3403
2010
Methanosarcina mazei, Methanosarcina mazei DSM 3647
brenda
McTernan, P.M.; Chandrayan, S.K.; Wu, C.H.; Vaccaro, B.J.; Lancaster, W.A.; Adams, M.W.
Engineering the respiratory membrane-bound hydrogenase of the hyperthermophilic archaeon Pyrococcus furiosus and characterization of the catalytically active cytoplasmic subcomplex
Protein Eng. Des. Sel.
28
1-8
2015
Pyrococcus furiosus (Q8U0Z8 and Q8U0Z7 and Q8U0Z6), Pyrococcus furiosus
brenda
Rumpel, S.; Siebel, J.F.; Diallo, M.; Fares, C.; Reijerse, E.J.; Lubitz, W.
Structural insight into the complex of ferredoxin and [FeFe] Hydrogenase from Chlamydomonas reinhardtii
ChemBioChem
16
1663-1669
2015
Chlamydomonas reinhardtii
brenda
Kim, E.; Tong, X.; Lee, J.
The ferredoxin Rr-HydB is required for the H2-evolving activity of Rr-HydA, a [FeFe]-hydrogenase of Rhodospirillum rubrum
Int. J. Hydrogen Energy
40
4320-4328
2015
Rhodospirillum rubrum, Rhodospirillum rubrum UR1
-
brenda
Zheng, Y.; Kahnt, J.; Kwon, I.H.; Mackie, R.I.; Thauer, R.K.
Hydrogen formation and its regulation in Ruminococcus albus involvement of an electron-bifurcating [FeFe]-hydrogenase, of a non-electron-bifurcating [FeFe]-hydrogenase, and of a putative hydrogen-sensing [FeFe]-hydrogenase
J. Bacteriol.
196
3840-3852
2014
Ruminococcus albus
brenda
McTernan, P.M.; Chandrayan, S.K.; Wu, C.H.; Vaccaro, B.J.; Lancaster, W.A.; Yang, Q.; Fu, D.; Hura, G.L.; Tainer, J.A.; Adams, M.W.
Intact functional fourteen-subunit respiratory membrane-bound [NiFe]-hydrogenase complex of the hyperthermophilic archaeon Pyrococcus furiosus
J. Biol. Chem.
289
19364-19372
2014
Pyrococcus furiosus, Pyrococcus furiosus COM1
brenda
Kosem, N.; Honda, Y.; Watanabe, M.; Takagaki, A.; Tehrani, Z.; Haydous, F.; Lippert, T.; Ishihara, T.
Photobiocatalytic H2 evolution of GaN ZnO and [FeFe]-hydrogenase recombinant Escherichia coli
Catal. Sci. Technol.
10
4042-4052
2020
Clostridium acetobutylicum, Clostridium acetobutylicum NBRC 13948
-
brenda
Rumpel, S.; Ravera, E.; Sommer, C.; Reijerse, E.; Fars, C.; Luchinat, C.; Lubitz, W.
1H NMR Spectroscopy of [FeFe] hydrogenase insight into the electronic structure of the active site
J. Am. Chem. Soc.
140
131-134
2018
Chlamydomonas reinhardtii (Q9FYU1), Chlamydomonas reinhardtii
brenda
Eckert, C.A.; Freed, E.; Wawrousek, K.; Smolinski, S.; Yu, J.; Maness, P.C.
Inactivation of the uptake hydrogenase in the purple non-sulfur photosynthetic bacterium Rubrivivax gelatinosus CBS enables a biological water-gas shift platform for H2 production
J. Ind. Microbiol. Biotechnol.
46
993-1002
2019
Rubrivivax gelatinosus, Rubrivivax gelatinosus CBS
brenda
Hardt, S.; Stapf, S.; Filmon, D.T.; Birrell, J.A.; Ruediger, O.; Fourmond, V.; Leger, C.; Plumere, N.
Reversible H2 oxidation and evolution by hydrogenase embedded in a redox polymer film
Nat. Catal.
4
251-258
2021
Desulfovibrio desulfuricans
brenda