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2 ferricyanide + NAD(P)H
2 ferrocyanide + NAD(P)+ + H+
ferrocyanide + NAD(P)H
ferricyanide + NAD(P)+
-
enzyme complex including HoxI
-
-
?
ferrocyanide + NAD+
ferricyanide + NADH
H+ + NADH + reduced ferredoxin
H2 + NAD+ + oxidized ferredoxin
H+ + NADPH
H2 + NADP+
-
-
-
-
?
H+ + reduced dithionite
H2 + oxidized dithionite
H+ + reduced methyl viologen
H2 + oxidized methyl viologen
H2 + acceptor
H+ + reduced acceptor
H2 + ferricyanide
H+ + ferrocyanide
H2 + ferrocyanide
H+ + ferricyanide
-
-
-
-
r
H2 + NAD(P)+
H+ + NAD(P)H
-
-
-
r
H2 + oxidized benzyl viologen
H+ + reduced benzyl viologen
H2 + oxidized benzyl viologen
reduced benzyl viologen + H+
H2 + oxidized dithionite
H+ + reduced dithionite
-
-
-
r
H2 + oxidized methyl viologen
H+ + reduced methyl viologen
H2 + oxidized methyl viologen
reduced methyl viologen + H+
H2 + oxidized methylene blue
H+ + reduced methylene blue
NAD(P)H + H+ + oxidized 2,6-dichlorophenolindophenol
NAD(P)+ + reduced 2,6-dichlorophenolindophenol
NAD+ + H+ + e-
NADH
-
diaphorase reaction part
-
-
r
NADH + K3Fe(CN)6
?
-
-
-
-
?
NADH + oxidized 2,6-dichlorophenol indophenol
NAD+ + reduced 2,6-dichlorophenol indophenol
NADH + oxidized benzyl viologen
NAD+ + reduced benzyl viologen
-
-
-
-
r
NADH + reduced 3-acetylpyridine adenine dinucleotide
NAD+ + oxidized 3-acetylpyridine adenine dinucleotide
NADPH + K3Fe(CN)6
?
-
low reaction with hexameric enzyme form, no reaction with tetrameric enzyme form
-
-
?
oxidized benzyl viologen + NADH
reduced benzyl viologen + NAD+
oxidized cytochrome c + NAD(P)H
reduced cytchrome c + NAD(P)+
-
-
-
?
oxidized methylene blue + NAD(P)H
reduced methylene blue + NAD(P)+
-
-
-
?
additional information
?
-
2 ferricyanide + NAD(P)H

2 ferrocyanide + NAD(P)+ + H+
-
-
-
?
2 ferricyanide + NAD(P)H
2 ferrocyanide + NAD(P)+ + H+
-
-
-
?
2 ferricyanide + NAD(P)H
2 ferrocyanide + NAD(P)+ + H+
-
-
-
?
2 ferricyanide + NAD(P)H
2 ferrocyanide + NAD(P)+ + H+
-
-
-
-
2 ferricyanide + NAD(P)H
2 ferrocyanide + NAD(P)+ + H+
-
-
-
?
2 ferricyanide + NAD(P)H
2 ferrocyanide + NAD(P)+ + H+
-
-
-
?
2 ferricyanide + NAD(P)H
2 ferrocyanide + NAD(P)+ + H+
-
-
-
?
2 ferricyanide + NAD(P)H
2 ferrocyanide + NAD(P)+ + H+
-
-
-
?
2 ferricyanide + NAD(P)H
2 ferrocyanide + NAD(P)+ + H+
-
-
-
?
ferrocyanide + NAD+

ferricyanide + NADH
-
-
-
-
r
ferrocyanide + NAD+
ferricyanide + NADH
-
diaphorase activity
-
-
r
ferrocyanide + NAD+
ferricyanide + NADH
-
-
-
-
r
H+ + NADH

H2 + NAD+
module HoxFU shows clear electrocatalytic activity for both NAD+ reduction and NADH oxidation with minimal overpotential relative to the potential of the NAD+/NADH couple
-
-
r
H+ + NADH
H2 + NAD+
module HoxFU shows clear electrocatalytic activity for both NAD+ reduction and NADH oxidation with minimal overpotential relative to the potential of the NAD+/NADH couple
-
-
r
H+ + NADH
H2 + NAD+
-
-
-
-
?
H+ + NADH + reduced ferredoxin

H2 + NAD+ + oxidized ferredoxin
-
the enzyme simultaneously uses electrons from NADH and reduced ferredoxin to produce hydrogen
-
-
?
H+ + NADH + reduced ferredoxin
H2 + NAD+ + oxidized ferredoxin
-
the enzyme simultaneously uses electrons from NADH and reduced ferredoxin to produce hydrogen
-
-
?
H+ + NADH + reduced ferredoxin
H2 + NAD+ + oxidized ferredoxin
-
bifurcating [FeFe]-hydrogenase in Syntrophobacter fumaroxidans simultaneously uses electrons from NADH and reduced ferredoxin in a 1:2 ratio to produce hydrogen
-
-
?
H+ + NADH + reduced ferredoxin
H2 + NAD+ + oxidized ferredoxin
-
bifurcating [FeFe]-hydrogenase in Syntrophobacter fumaroxidans simultaneously uses electrons from NADH and reduced ferredoxin in a 1:2 ratio to produce hydrogen
-
-
?
H+ + NADH + reduced ferredoxin
H2 + NAD+ + oxidized ferredoxin
-
the hydrogenase requires the presence of both electron carriers, NADH and reduced ferredoxin, synergistically in a 1:1 ratio for catalysis of H2 production
-
-
?
H+ + NADH + reduced ferredoxin
H2 + NAD+ + oxidized ferredoxin
-
the hydrogenase requires the presence of both electron carriers, NADH and reduced ferredoxin, synergistically in a 1:1 ratio for catalysis of H2 production
-
-
?
H+ + reduced dithionite

H2 + oxidized dithionite
-
-
-
-
?
H+ + reduced dithionite
H2 + oxidized dithionite
-
-
-
-
?
H+ + reduced dithionite
H2 + oxidized dithionite
-
-
-
-
?
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
-
-
-
-
?
H2

H+ + e-
-
hydrogenase reaction part
-
-
r
H2
H+ + e-
-
hydrogenase reaction part
-
-
r
H2 + acceptor

H+ + reduced acceptor
-
-
-
-
?
H2 + acceptor
H+ + reduced acceptor
-
-
-
-
?
H2 + acceptor
H+ + reduced acceptor
-
-
-
-
?
H2 + ferricyanide

H+ + ferrocyanide
-
1257% activity compared to electron acceptor NAD+
-
?
H2 + ferricyanide
H+ + ferrocyanide
-
585% activity compared to electron acceptor NAD+
-
?
H2 + ferricyanide
H+ + ferrocyanide
-
1257% activity compared to electron acceptor NAD+
-
?
H2 + ferricyanide
H+ + ferrocyanide
-
389% activity compared to electron acceptor NAD+
-
?
H2 + ferricyanide
H+ + ferrocyanide
-
-
-
-
r
H2 + ferricyanide
H+ + ferrocyanide
-
708% activity compared to electron acceptor NAD+
-
?
H2 + ferricyanide
H+ + ferrocyanide
-
708% activity compared to electron acceptor NAD+
-
?
H2 + ferricyanide
H+ + ferrocyanide
-
708% activity compared to electron acceptor NAD+
-
?
H2 + ferricyanide
H+ + ferrocyanide
-
-
-
-
r
H2 + ferricyanide
H+ + ferrocyanide
-
350% activity compared to electron acceptor NAD+
-
?
H2 + NAD+

H+ + NADH
-
-
-
-
?
H2 + NAD+
H+ + NADH
-
-
-
-
?
H2 + NAD+
H+ + NADH
-
-
-
-
?
H2 + NAD+
H+ + NADH
-
-
-
-
r
H2 + NAD+
H+ + NADH
-
electron transfer between the catalytic site for NADH-oxidation and the hydrogenase catalytic site is rate-limiting
-
-
r
H2 + NAD+
H+ + NADH
-
-
-
-
H2 + NAD+
H+ + NADH
-
-
-
-
H2 + NAD+
H+ + NADH
-
-
-
-
H2 + NAD+
H+ + NADH
-
-
-
-
H2 + NAD+
H+ + NADH
-
-
-
-
H2 + NAD+
H+ + NADH
-
-
-
-
H2 + NAD+
H+ + NADH
-
-
-
-
H2 + NAD+
H+ + NADH
-
-
-
-
H2 + NAD+
H+ + NADH
-
-
-
-
H2 + NAD+
H+ + NADH
-
-
-
-
H2 + NAD+
H+ + NADH
-
-
-
-
H2 + NAD+
H+ + NADH
-
-
-
-
H2 + NAD+
H+ + NADH
-
-
-
-
H2 + NAD+
H+ + NADH
-
-
-
-
H2 + NAD+
H+ + NADH
-
-
-
-
?
H2 + NAD+
H+ + NADH
-
-
-
-
r
H2 + NAD+
H+ + NADH
-
electron acceptor FMN
-
r
H2 + NAD+
H+ + NADH
-
electron acceptor FAD
-
r
H2 + NAD+
H+ + NADH
-
no activity with NADP+
-
-
r
H2 + NAD+
H+ + NADH
-
artificial electron acceptors: Janus green, 2,6-dichlorophenolindophenol, phenazine methosulfate, menaquinone, ubiquinone, cytochrome c
-
r
H2 + NAD+
H+ + NADH
-
hydrogenase produces superoxide free radical anions, which are responsible for enzyme inactivation
-
-
H2 + NAD+
H+ + NADH
-
artificial electron acceptor benzyl viologen
-
r
H2 + NAD+
H+ + NADH
-
artificial electron acceptor methyl viologen
-
r
H2 + NAD+
H+ + NADH
-
weak electron acceptor O2
-
r
H2 + NAD+
H+ + NADH
-
enzyme also has diaphorase and NAD(P)H oxidase activity
-
r
H2 + NAD+
H+ + NADH
-
electron acceptor NAD+
-
r
H2 + NAD+
H+ + NADH
-
artificial electron acceptor ferricyanide
-
r
H2 + NAD+
H+ + NADH
-
artificial electron acceptor resazurin
-
-
H2 + NAD+
H+ + NADH
-
artificial electron acceptor methylene blue
-
r
H2 + NAD+
H+ + NADH
-
utilization of H2 as energy source during autotrophic growth on hydrogen and CO2
-
r
H2 + NAD+
H+ + NADH
-
utilization of H2 as energy source during autotrophic growth on hydrogen and CO2
-
r
H2 + NAD+
H+ + NADH
-
enzyme provides reducing equivalents for CO2 fixation
-
-
r
H2 + NAD+
H+ + NADH
-
key enzyme in H2 metabolism
-
-
r
H2 + NAD+
H+ + NADH
-
H2 activation solely takes place on Ni2+
-
-
r
H2 + NAD+
H+ + NADH
-
overall reaction
-
-
r
H2 + NAD+
H+ + NADH
-
the enzyme catalyzes electron transfer from molecular hydrogen to NAD+, thereby producing reducing equivalents for CO2 fixation in the form of NADH
-
-
?
H2 + NAD+
H+ + NADH
module HoxFU shows clear electrocatalytic activity for both NAD+ reduction and NADH oxidation with minimal overpotential relative to the potential of the NAD+/NADH couple
-
-
r
H2 + NAD+
H+ + NADH
-
-
-
-
H2 + NAD+
H+ + NADH
-
-
-
-
H2 + NAD+
H+ + NADH
module HoxFU shows clear electrocatalytic activity for both NAD+ reduction and NADH oxidation with minimal overpotential relative to the potential of the NAD+/NADH couple
-
-
r
H2 + NAD+
H+ + NADH
-
-
-
-
H2 + NAD+
H+ + NADH
-
-
-
-
H2 + NAD+
H+ + NADH
-
utilization of H2 as energy source during autotrophic growth on hydrogen and CO2
-
r
H2 + NAD+
H+ + NADH
-
-
-
-
H2 + NAD+
H+ + NADH
-
electron acceptor FMN
-
r
H2 + NAD+
H+ + NADH
-
electron acceptor FAD
-
r
H2 + NAD+
H+ + NADH
-
artificial electron acceptors: Janus green, 2,6-dichlorophenolindophenol, phenazine methosulfate, menaquinone, ubiquinone, cytochrome c
-
r
H2 + NAD+
H+ + NADH
-
-
-
-
H2 + NAD+
H+ + NADH
-
-
-
-
H2 + NAD+
H+ + NADH
-
hydrogenase produces superoxide free radical anions, which are responsible for enzyme inactivation
-
-
H2 + NAD+
H+ + NADH
-
-
-
-
H2 + NAD+
H+ + NADH
-
-
-
-
r
H2 + NAD+
H+ + NADH
-
no activity with NADP+
-
-
r
H2 + NAD+
H+ + NADH
-
key enzyme in H2 metabolism
-
-
r
H2 + NAD+
H+ + NADH
-
-
-
-
?
H2 + NAD+
H+ + NADH
-
overall reaction
-
-
r
H2 + NAD+
H+ + NADH
-
-
-
-
H2 + NAD+
H+ + NADH
-
-
-
-
H2 + NAD+
H+ + NADH
-
artificial electron acceptor resazurin
-
-
H2 + NAD+
H+ + NADH
-
-
-
-
H2 + NAD+
H+ + NADH
-
-
-
-
H2 + NAD+
H+ + NADH
-
-
-
-
r
H2 + NAD+
H+ + NADH
-
physiological function of the enzyme in Frankia strains, overview
-
-
r
H2 + NAD+
H+ + NADH
-
-
-
r
H2 + NAD+
H+ + NADH
H2 producing activity is not dependent on NAD+ reduction
-
-
r
H2 + NAD+
H+ + NADH
-
only 3-8% of the benzyl biologen or methyl viologen-dependent values. The enzyme interacts with NADP+ and NADPH, but is more specific to NAD+ and NADH
-
-
r
H2 + NAD+
H+ + NADH
-
only 3-8% of the benzyl biologen or methyl viologen-dependent values. The enzyme interacts with NADP+ and NADPH, but is more specific to NAD+ and NADH
-
-
r
H2 + NAD+
H+ + NADH
Hydrogenomonas sp.
-
electron acceptor FAD, only in presence of catalytic amounts of NAD+
-
?
H2 + NAD+
H+ + NADH
Hydrogenomonas sp.
-
artificial electron acceptor methylene blue, only in presence of catalytic amounts of NAD+
-
?
H2 + NAD+
H+ + NADH
Hydrogenomonas sp.
-
electron acceptor FMN, only in presence of catalytic amounts of NAD+
-
?
H2 + NAD+
H+ + NADH
-
electron acceptor FAD, only in presence of catalytic amounts of NAD+
-
?
H2 + NAD+
H+ + NADH
-
artificial electron acceptor methylene blue, only in presence of catalytic amounts of NAD+
-
?
H2 + NAD+
H+ + NADH
-
electron acceptor FMN, only in presence of catalytic amounts of NAD+
-
?
H2 + NAD+
H+ + NADH
-
-
-
-
r
H2 + NAD+
H+ + NADH
-
enzyme delivers hydrogen-driven reducing power for methane oxidation
-
-
r
H2 + NAD+
H+ + NADH
-
-
-
-
H2 + NAD+
H+ + NADH
-
-
-
-
-
H2 + NAD+
H+ + NADH
-
-
-
-
r
H2 + NAD+
H+ + NADH
-
electron acceptor FAD
-
r
H2 + NAD+
H+ + NADH
-
artificial electron acceptor benzyl viologen
-
-
H2 + NAD+
H+ + NADH
-
artificial electron acceptor benzyl viologen
-
r
H2 + NAD+
H+ + NADH
-
artificial electron acceptor methyl viologen
-
-
H2 + NAD+
H+ + NADH
-
artificial electron acceptor methyl viologen
-
r
H2 + NAD+
H+ + NADH
-
electron acceptor NAD+
-
-
H2 + NAD+
H+ + NADH
-
electron acceptor NAD+
-
r
H2 + NAD+
H+ + NADH
-
artificial electron acceptor ferricyanide
-
r
H2 + NAD+
H+ + NADH
-
artificial electron acceptor methylene blue, only in presence of catalytic amounts of NAD+
-
-
H2 + NAD+
H+ + NADH
-
artificial electron acceptor methylene blue
-
-
H2 + NAD+
H+ + NADH
-
artificial electron acceptor methylene blue
-
r
H2 + NAD+
H+ + NADH
-
artificial electron acceptor benzyl viologen
-
-
H2 + NAD+
H+ + NADH
-
artificial electron acceptor methyl viologen
-
-
H2 + NAD+
H+ + NADH
-
electron acceptor NAD+
-
-
H2 + NAD+
H+ + NADH
-
artificial electron acceptor methylene blue, only in presence of catalytic amounts of NAD+
-
-
H2 + NAD+
H+ + NADH
-
artificial electron acceptor methylene blue
-
-
H2 + NAD+
H+ + NADH
-
electron acceptor FAD
-
r
H2 + NAD+
H+ + NADH
-
artificial electron acceptor benzyl viologen
-
r
H2 + NAD+
H+ + NADH
-
artificial electron acceptor methyl viologen
-
r
H2 + NAD+
H+ + NADH
-
electron acceptor NAD+
-
r
H2 + NAD+
H+ + NADH
-
-
-
-
H2 + NAD+
H+ + NADH
-
-
-
-
r
H2 + NAD+
H+ + NADH
-
-
-
r
H2 + NAD+
H+ + NADH
-
-
-
-
?
H2 + NAD+
H+ + NADH
-
-
-
r
H2 + NAD+
H+ + NADH
in vivo H2 evolution under nitrogenase-repressed conditions
-
-
r
H2 + NAD+
H+ + NADH
-
-
-
-
?
H2 + NADP+

H+ + NADPH
-
only 3-8% of the benzyl biologen or methyl viologen-dependent values. The enzyme interacts with NADP+ and NADPH, but is more specific to NAD+ and NADH
-
-
r
H2 + NADP+
H+ + NADPH
-
only 3-8% of the benzyl biologen or methyl viologen-dependent values. The enzyme interacts with NADP+ and NADPH, but is more specific to NAD+ and NADH
-
-
r
H2 + oxidized benzyl viologen

H+ + reduced benzyl viologen
-
-
-
-
?
H2 + oxidized benzyl viologen
H+ + reduced benzyl viologen
-
-
-
r
H2 + oxidized benzyl viologen
H+ + reduced benzyl viologen
-
-
-
-
r
H2 + oxidized benzyl viologen
H+ + reduced benzyl viologen
-
hydrogenase activity
-
-
r
H2 + oxidized benzyl viologen
H+ + reduced benzyl viologen
-
-
-
-
r
H2 + oxidized benzyl viologen
H+ + reduced benzyl viologen
-
-
-
-
r
H2 + oxidized benzyl viologen
H+ + reduced benzyl viologen
-
50fold higher specific activity compared to NAD+ reduction
-
r
H2 + oxidized benzyl viologen
H+ + reduced benzyl viologen
-
-
-
-
r
H2 + oxidized benzyl viologen

reduced benzyl viologen + H+
-
-
-
-
?
H2 + oxidized benzyl viologen
reduced benzyl viologen + H+
-
-
-
-
?
H2 + oxidized benzyl viologen
reduced benzyl viologen + H+
-
-
-
-
?
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
-
-
-
-
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
-
-
-
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
-
-
-
r
H2 + oxidized methyl viologen
H+ + reduced methyl viologen
the artificial electron donor is accepted by the cells for H2 production when added to the culture medium
-
-
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
-
-
-
?
H2 + oxidized methyl viologen
H+ + reduced methyl viologen
-
-
-
-
-
H2 + oxidized methyl viologen
H+ + reduced methyl viologen
-
-
-
-
?
H2 + oxidized methyl viologen
H+ + reduced methyl viologen
-
best cofactor
-
r
H2 + oxidized methyl viologen
H+ + reduced methyl viologen
-
-
-
r
H2 + oxidized methyl viologen

reduced methyl viologen + H+
-
-
-
-
r
H2 + oxidized methyl viologen
reduced methyl viologen + H+
-
-
-
-
r
H2 + oxidized methylene blue

H+ + reduced methylene blue
-
-
-
?
H2 + oxidized methylene blue
H+ + reduced methylene blue
-
-
-
?
H2 + oxidized methylene blue
H+ + reduced methylene blue
-
-
-
?
H2 + oxidized methylene blue
H+ + reduced methylene blue
-
-
-
?
H2 + oxidized methylene blue
H+ + reduced methylene blue
-
-
-
?
H2 + oxidized methylene blue
H+ + reduced methylene blue
-
-
-
?
H2 + oxidized methylene blue
H+ + reduced methylene blue
-
-
-
-
r
H2 + oxidized methylene blue
H+ + reduced methylene blue
-
-
-
?
H2 + oxidized methylene blue
H+ + reduced methylene blue
-
-
-
r
NAD(P)H + H+ + oxidized 2,6-dichlorophenolindophenol

NAD(P)+ + reduced 2,6-dichlorophenolindophenol
-
-
-
?
NAD(P)H + H+ + oxidized 2,6-dichlorophenolindophenol
NAD(P)+ + reduced 2,6-dichlorophenolindophenol
-
-
-
?
NADH + oxidized 2,6-dichlorophenol indophenol

NAD+ + reduced 2,6-dichlorophenol indophenol
-
-
-
-
?
NADH + oxidized 2,6-dichlorophenol indophenol
NAD+ + reduced 2,6-dichlorophenol indophenol
-
-
-
-
?
NADH + reduced 3-acetylpyridine adenine dinucleotide

NAD+ + oxidized 3-acetylpyridine adenine dinucleotide
-
-
-
-
?
NADH + reduced 3-acetylpyridine adenine dinucleotide
NAD+ + oxidized 3-acetylpyridine adenine dinucleotide
-
-
-
-
?
oxidized benzyl viologen + NADH

reduced benzyl viologen + NAD+
-
-
-
?
oxidized benzyl viologen + NADH
reduced benzyl viologen + NAD+
-
-
-
?
additional information

?
-
-
at high H2 partial pressure enzyme activity is reduced and fermentation is partially shifted to ethanol production
-
-
-
additional information
?
-
-
enzyme autoxidation
-
-
-
additional information
?
-
-
activity is equally high in atmosperes of 20% O2, 20% N2, or 100% H2, the latter being slightly preferred
-
-
-
additional information
?
-
-
enzyme regulation involves a regulatory hydrogenase RH which acts as a sensor for H2 content, interaction via signal cascade
-
-
-
additional information
?
-
-
the organism can grow on H2 as sole energy source in an oxic environment
-
-
-
additional information
?
-
-
addition of NADH prolonged the lag phase before H2 consumption
-
-
-
additional information
?
-
-
deuterium-hydrogen proton exchange activity of wild-type and mutantenzymes, overview
-
-
-
additional information
?
-
-
enzyme shows both hydrogenase and diaphorase activities, proton channeling
-
-
-
additional information
?
-
-
FMN release induces reduction with NADH, enzyme shows both hydrogenase and diaphorase activities, proton channeling
-
-
-
additional information
?
-
-
tetrameric or hexameric enzyme form: no H2 production from NADPH
-
-
-
additional information
?
-
in protein film electrochemical experiments the electrocatalytic current is unaffected by O2. In aerobic solution assays, a moderate superoxide production rate of 54 nmol per mg of protein is observed, meaning that the formation of reactive oxygen species observed for the native enzyme can be attributed mainly to module HoxFU
-
-
-
additional information
?
-
in protein film electrochemical experiments the electrocatalytic current is unaffected by O2. In aerobic solution assays, a moderate superoxide production rate of 54 nmol per mg of protein is observed, meaning that the formation of reactive oxygen species observed for the native enzyme can be attributed mainly to module HoxFU
-
-
-
additional information
?
-
in protein film electrochemical experiments the electrocatalytic current is unaffected by O2. In aerobic solution assays, a moderate superoxide production rate of 54 nmol per mg of protein is observed, meaning that the formation of reactive oxygen species observed for the native enzyme can be attributed mainly to module HoxFU
-
-
-
additional information
?
-
in protein film electrochemical experiments the electrocatalytic current is unaffected by O2. In aerobic solution assays, a moderate superoxide production rate of 54 nmol per mg of protein is observed, meaning that the formation of reactive oxygen species observed for the native enzyme can be attributed mainly to module HoxFU
-
-
-
additional information
?
-
-
the organism can grow on H2 as sole energy source in an oxic environment
-
-
-
additional information
?
-
-
tetrameric or hexameric enzyme form: no H2 production from NADPH
-
-
-
additional information
?
-
-
enzyme shows both hydrogenase and diaphorase activities, proton channeling
-
-
-
additional information
?
-
enzyme is the key enzyme in hydrogen metabolism, no activity in strain R43 under aerobic nitrogen-limited conditions
-
-
-
additional information
?
-
enzyme is the key enzyme in hydrogen metabolism, no activity in strain R43 under aerobic nitrogen-limited conditions
-
-
-
additional information
?
-
enzyme is the key enzyme in hydrogen metabolism, no activity in strain R43 under aerobic nitrogen-limited conditions
-
-
-
additional information
?
-
enzyme is the key enzyme in hydrogen metabolism, no activity in strain R43 under aerobic nitrogen-limited conditions
-
-
-
additional information
?
-
-
physiological role of the hydrogenase seems to be equally associated with both formation and uptake of H2, depending on the redox state of the intracellular medium
-
-
-
additional information
?
-
-
physiological role of the hydrogenase seems to be equally associated with both formation and uptake of H2, depending on the redox state of the intracellular medium
-
-
-
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Co2+
-
NAD+ reduction with H2 is completely dependent on the presence of divalent metal ions Ni2+, Co2+, Mg2+ or Mn2+ or of high salt concentrations between 500-1500 mM
cyanide
-
enzyme contains four cyanides in its active site, one of which is responsible for the insensitivity towards oxygen
Nickel
-
[NiFe] hydrogenases carry a metal centre composed of Fe and Ni atoms at the active site
CN-

-
enzyme contains four cyanides in its active site, one is bound to the Ni2+, the active site is a (enzyme-Cys)2(CN)Ni(micro-enzyme-Cys)2Fe(CN)3(CO) centre, the CN- bound to the nickel ion can be irreversibly removed inducing enzyme inhibition by oxygen
CN-
-
enzyme contains four cyanides in its active site, the Ni2+ bound one is responsible for the insensitivity towards oxygen, the active site is a (enzyme-Cys)2(CN)Ni(micro-enzyme-Cys)2Fe(CN)3(CO) centre, the CN- bound to the nickel ion can be irreversibly removed inducing enzyme inhibition by oxygen
CO

-
the active site is a (enzyme-Cys)2(CN)Ni(micro-enzyme-Cys)2Fe(CN)3(CO) centre
CO
-
bound to the active site, the active site is a (enzyme-Cys)2(CN)Ni(micro-enzyme-Cys)2Fe(CN)3(CO) centre
Fe

-
Ni-Fe hydrogenase. Monitoring of the structure and oxidation state of its metal centers during H2 turnover
Fe
-
Ni-Fe enzyme. Analysis of the Ni-Fe cofactor revealed a nonstandard structure, (CN)(O)3NiII(mu-CysS)2FeII(CN)3(CO)
Fe
-
the (CO)3Fe(II) site is octahedral. An octahedral iron and a distorted square pyramidal nickel are linked by three bridging ligands
Fe2+

-
the active site is a (enzyme-Cys)2(CN)Ni(micro-enzyme-Cys)2Fe(CN)3(CO) centre
Fe2+
-
enzyme contains a [Ni-Fe] cluster; the active site is a (enzyme-Cys)2(CN)Ni(micro-enzyme-Cys)2Fe(CN)3(CO) centre
Fe2+
-
contains iron in the catalytic core
Iron

-
enzyme contains multiple iron-sulfur clusters, [4Fe-4S] or [2Fe-2S]
Iron
-
no increase of activity by addition of Co2+, Mn2+, Ni2+ or Fe2+; non-heme iron protein
Iron
-
non-heme iron protein
Iron
-
11.5 iron atoms per enzyme molecule, enzyme contains 2 [4Fe-4S] and 2 [2Fe-2S] clusters
Iron
-
the diaphorase contains 3 [2Fe-2S] cluster, the hydrogenase subunit HoxY contains one [2Fe-2S] cluster coordinated by 9 Cys residues
Iron
the active site iron atom has a standard ligation, i.e., one CO and two cyanide ligands; the active site iron atom has a standard ligation, i.e., one CO and two cyanide ligands
Iron
Hydrogenomonas sp.
-
Fe2+ stabilizes
Iron
-
13.6 iron atoms per enzyme molecule; non-heme iron protein
Iron
-
the enzyme contains at least one [4Fe4S]+ and at least one [2Fe2S]+ cluster
Iron
-
[NiFe] hydrogenases carry a metal centre composed of Fe and Ni atoms at the active site
Mg2+

-
bound to the hydrogenase subunits
Mg2+
Hydrogenomonas sp.
-
stabilizes
Mg2+
-
NAD-reduction: no linear kinetics in absence of metals, 0.5 mM Ni2+ and 5 mM Mg2+ required
Mg2+
-
NAD+ reduction with H2 is completely dependent on the presence of divalent metal ions Ni2+, Co2+, Mg2+ or Mn2+ or of high salt concentrations between 500-1500 mM
Mn2+

Hydrogenomonas sp.
-
stabilizes
Mn2+
-
NAD+ reduction with H2 is completely dependent on the presence of divalent metal ions Ni2+, Co2+, Mg2+ or Mn2+, or of high salt concentrations of 500-1500 mM
Ni

-
Ni-Fe hydrogenase. Monitoring of the structure and oxidation state of its metal centers during H2 turnover
Ni
-
Ni-Fe enzyme. Analysis of the Ni-Fe cofactor revealed a nonstandard structure, (CN)(O)3NiII(mu-CysS)2FeII(CN)3(CO). The unusual ligation of the Ni by only two thiols plus further (C,O) ligands seems to be a prerequisite of the exceptionally rapid activation of the SH by NADH, involving the loss of an oxygen ligand from the Ni. Evidence for the binding of hydrogen to the open coordination site at Ni has been obtained. The hydrogen cleavage reaction seems not to involve a Ni-C state (Ni(III)-H-). The CN ligand at the Ni may be involved in establishing both rapid activation and oxygen-insensitive catalytic behavior in the SH. Possibly, one important function of the CN is stabilization of the Ni(II) oxidation state throughout the catalytic cycle of hydrogen cleavage
Ni2+

-
below 0.06 mol Ni2+ per mol of enzyme
Ni2+
-
nickel is essential for the catalytic activity of the enzyme
Ni2+
-
2 nickel atoms per enzyme molecule; nickel is essential for the catalytic activity of the enzyme
Ni2+
-
presence of a Ni(CN)Fe(CN)3(CO) active site is suggested
Ni2+
-
the active site is a (enzyme-Cys)2(CN)Ni(micro-enzyme-Cys)2Fe(CN)3(CO) centre, H2 activation solely takes place on Ni2+
Ni2+
-
enzyme contains a [Ni-Fe] cluster
Ni2+
-
the active site is a (enzyme-Cys)2(CN)Ni(micro-enzyme-Cys)2Fe(CN)3(CO) centre
Ni2+
-
enzyme contains a [Ni-Fe] cluster; the active site is a (enzyme-Cys)2(CN)Ni(micro-enzyme-Cys)2Fe(CN)3(CO) centre, H2 activation solely takes place on Ni2+
Ni2+
-
contains nickel in the catalytic core
Ni2+
-
NAD-reduction: no linear kinetics in absence of metals, 0.5 mM Ni2+ and 5 mM Mg2+ required
Ni2+
-
highest specific activity with NiCl2, optimal concentration: 1 mM; NAD+ reduction with H2 is completely dependent on the presence of divalent metal ions Ni2+, Co2+, Mg2+ or Mn2+ or of high salt concentrations between 500-1500 mM
Ni2+
-
3.8 nickel atoms per enzyme molecule; nickel protein
Ni2+
-
take-up/release of substrates may occur at the Ni site. Flexible coordination structures at Ni may be responsible for the interconversion between H2 and (2H+) as the unique function of the [NiFe] hydrogenase. The coordination mode of the Ni(II) center can vary from square planar, to distorted square pyramidal, and to octahedral geometries, dependent on the nature of the ligands. An octahedral iron and a distorted square pyramidal nickel are linked by three bridging ligands
additional information

-
no increase of activity by addition of Co2+, Mn2+, Ni2+ or Fe2+
additional information
-
metalloenzyme
additional information
-
stimulation of activity by salt is greater the less chaotrophic the anion
additional information
metalloenzyme
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0.0017
-
soluble periplasmic fraction, hydrogen producing activity with electron acceptor oxidized methyl viologen
0.0018
cell culture in nitrogen-limited medium, anaerobic conditions, H2 production using reduced methyl viologen as electron donor
0.0029
-
soluble periplasmic fraction, hydrogen producing activity with electron donor NADH
0.006
-
soluble periplasmic fraction, hydrogen producing activity with electron donor reduced benzyl viologen
0.0095
-
soluble periplasmic fraction, hydrogen producing activity with electron acceptor oxidized benzyl viologen
0.0113
-
soluble periplasmic fraction, hydrogen producing activity with electron donor reduced methyl viologen
0.0175
-
soluble periplasmic fraction, hydrogen producing activity with electron acceptor oxidized methylene blue
0.0255
-
soluble periplasmic fraction, hydrogen producing activity with electron acceptor NAD+
0.035
-
H2 producing activity, strain R43 grown without nitrogen and nickel, from host plant Compotonia cunninghamiana, with reduced methyl viologen as electron donor
0.076
-
crude extract, pH and temperature not specified in the publication
0.11
-
H2 producing activity, strain UGL011101 grown without nitrogen and nickel, from host plant Alnus incana, with reduced methyl viologen as electron donor
0.3
-
H2 producing activity, strain HFPCcI3 grown without nitrogen and nickel, from host plant Compotonia cunninghamiana, with reduced methyl viologen as electron donor
1.7
-
recombinant enzyme expressed in Ralstonia eutropha
4.91
-
H2 producing activity, strain UGL140102 grown without nitrogen and nickel, from host plant Hippophae rhamnoides, with reduced methyl viologen as electron donor
5
-
purified enzyme, H2 consumption
5.6
-
strain Cd2/01, electron acceptor NAD+
7.7
-
electron acceptor NAD+
10
-
purified enzyme, H2 production
15
native purified enzyme complex from strain PCC 6301, hydrogen-forming activity, cofactor reduced methyl viologen
17 - 84
-
activity of different batches with NAD+ and H2
25.2
-
reaction with H2 and benzyl viologen, purified HoxI deletion mutant enzyme
30 - 100
-
purified enzyme, forward reaction under aerobic conditions with NAD+
34
-
electron acceptor NAD+
35.1
-
reaction with H2 and benzyl viologen, purified wild-type enzyme complex including HoxI
36.5
Hydrogenomonas sp.
-
-
38
-
strain H16, electron acceptor NAD+
39
-
reaction with H2 and NAD+, purified HoxI deletion mutant enzyme
41.9
-
reaction with H2 and NAD+, purified wild-type enzyme complex including HoxI
61.6
-
reaction with NADH and ferrocyanide, purified HoxI deletion mutant enzyme
64.9
-
reaction with NADH and ferrocyanide, purified wild-type enzyme complex including HoxI
67
native purified enzyme complex from strain PCC 6803, hydrogen-forming activity, cofactor reduced methyl viologen
72
-
electron acceptor NAD+
85
-
electron acceptor NAD+
87.78
-
after 1155old purification, pH and temperature not specified in the publication
100
-
electron acceptor benzyl viologen
102.1
-
reaction with H2 and ferrocyanide, purified HoxI deletion mutant enzyme
108.8
-
reaction with H2 and ferrocyanide, purified wild-type enzyme complex including HoxI
125 - 175
-
activity of different batches with NADH and ferricyanide
230
-
recombinant protein, pH 8.0, temperature not specified in the publication
1263
-
activity of different batches with benzyl viologen and H2
1300
-
purified enzyme, with substrates oxidized benzyl viologen and NADH
1700
-
purified enzyme, both reaction directions with substrates oxidized/reduced methyl viologen and H2/H+
2030
-
purified hydrogenase, at 30°C
0.0006

cell culture in nitrogen-enriched medium, anaerobic conditions, H2 production using reduced methyl viologen as electron donor
0.0006
-
soluble periplasmic fraction, hydrogen producing activity with electron donor reduced methylene blue
0.6

-
H2-evolution in vivo, fermenter-grown cells
0.6
-
reaction with NADPH and ferrocyanide, purified wild-type enzyme complex including HoxI, no reaction with the HoxI deletion mutant
additional information

-
-
additional information
-
-
additional information
-
-
additional information
-
no H2 producing activity in several strains grown without nitrogen and nickel, overview
additional information
H2-uptake activity at different conditions
additional information
H2-uptake activity at different conditions
additional information
H2-uptake activity at different conditions
additional information
H2-uptake activity at different conditions
additional information
-
hydrogen-driven methane monooxygenase activity in the soluble periplasmic fraction, overview
additional information
determination of H2 production rates in vivo
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?

-
x * 63000 + x * 30000 + x * 26000 + x * 56000, SDS-PAGE, deduced from nucleotide sequence
?
-
x * 63000 + x * 30000 + x * 26000 + x * 56000, SDS-PAGE, deduced from nucleotide sequence
-
?
x * 18000, HoxE, SDS-PAGE, x * 21000, recombinant HIs-tagged HoxE, SDS-PAGE
hexamer

-
subunit stoichiometry of HoxFUYI2. Subunit HoxIhas a MW of 19000 Da as determined by SDS-PAGE
hexamer
-
subunit stoichiometry of HoxFUYI2. Subunit HoxIhas a MW of 19000 Da as determined by SDS-PAGE
-
oligomer

-
heterotetrameric multifunctional enzyme showing both hydrogenase and diaphorase activities, subunits HoxHY form a heterodimer which is responsible for the hydrogenase activity with 56 kDa for HoxH and 26 kDa for HoxY, subunits HoxFU form a heterodimer which is responsible for the NADH-dehydrogenase, i.e. diaphorase activity
oligomer
-
enzyme is composed as a dimer of pentamers, the latter consisting of subunit pairs HoxU with HoxF, and HoxY with HoxH, and a fifth 19 kDa subunit HoxI, i.e. B protein, the HoxFU dimer is the NADH-dehydrogenase moiety, the HoxHY dimer is the hydrogenase moiety, overview
oligomer
-
enzyme is composed as a dimer of pentamers, the latter consisting of subunit pairs HoxU with HoxF, and HoxY with HoxH, and a fifth 19 kDa subunit HoxI, i.e. B protein, the HoxFU dimer is the NADH-dehydrogenase moiety, the HoxHY dimer is the hydrogenase moiety, overview; heterotetrameric multifunctional enzyme showing both hydrogenase and diaphorase activities, subunits HoxHY form a heterodimer which is responsible for the hydrogenase activity with 56 kDa for HoxH and 26 kDa for HoxY, subunits HoxFU form a heterodimer which is responsible for the NADH-dehydrogenase, i.e. diaphorase activity
-
tetramer

-
1 * 65000 + 1 * 64000 + 1 * 20000 + 1 * 14000, SDS-PAGE
tetramer
-
the catalytic subunit is termed HoxH
tetramer
-
1 * 67000 + 1 * 55000 + 1 * 26000 + 1 * 23000
tetramer
-
enzyme is composed of 4 Hox subunits, HoxF, HoxH, HoxU, and HoxY, with MWs of 67 kDa, 55 kDa, 26 kDa, and 23 kDa
tetramer
-
1 * 64000 + 1 * 56000 + 1 * 31000 + 1 * 27000, native hydrogenase dissociates into two subunit dimers of 64000 Da and 1 * 31000 Da, and of 56000 Da and 27000 Da respectively, SDS-PAGE
tetramer
-
1 * 64000 + 1 * 56000 + 1 * 31000 + 1 * 27000, native hydrogenase dissociates into two subunit dimers of 64000 Da and 1 * 31000 Da, and of 56000 Da and 27000 Da respectively, SDS-PAGE
-
additional information

-
enzyme is composed of 4 subunits
additional information
-
enzyme is composed of 4 subunits
-
additional information
-
enzyme is composed of 4 subunits
additional information
-
structure analysis and subunit composition, HoxI is associated with the NADH-dehydrogenase moiety of the enzyme
additional information
-
subunits HoxHY form a heterodimer which is responsible for the hydrogenase activity, subunits HoxFU form a heterodimer which is responsible for the NADH-dehydrogenase or diaphorase activity
additional information
-
use of a reverse micelle system for study of oligomeric structure
additional information
-
structure analysis and subunit composition, HoxI is associated with the NADH-dehydrogenase moiety of the enzyme; use of a reverse micelle system for study of oligomeric structure
-
additional information
-
large dimer composed of 64000 Da and 31000 Da subunit contains 1 FMN, 1 [2Fe-2S] and 2 [4Fe-4S] cluster, diaphorase activity is located on large dimer, small dimer composed of 56000 Da and 27000 Da subunits contains 2 Ni and 1 [4Fe-4S]/[3Fe-xS] cluster, hydrogenase activity is localized on small dimer
additional information
-
enzyme is composed of 4 subunits
additional information
-
in low-salt buffer the tetrameric enzyme dissociates into 2 dimeric forms accompanied by the failure to reduce NAD+
additional information
-
large dimer composed of 64000 Da and 31000 Da subunit contains 1 FMN, 1 [2Fe-2S] and 2 [4Fe-4S] cluster, diaphorase activity is located on large dimer, small dimer composed of 56000 Da and 27000 Da subunits contains 2 Ni and 1 [4Fe-4S]/[3Fe-xS] cluster, hydrogenase activity is localized on small dimer
-
additional information
-
in low-salt buffer the tetrameric enzyme dissociates into 2 dimeric forms accompanied by the failure to reduce NAD+
-
additional information
the subunit HoxE, which is essential for the bidirectional hydrogenase activity, is included in a pentameric bidirectional hydrogenase complex HoxEFUYH in cyanobacteria, the complex forms dimer (HoxEFUYH)2, complex components are HoxE, HoxF, HoxH, HoxU, and HoxY, complex composition analysis, overview
additional information
the subunit HoxE, which is essential for the bidirectional hydrogenase activity, is included in a pentameric bidirectional hydrogenase complex HoxEFUYH of the cyanobacterial-type, complex components are HoxE, HoxF, HoxH, HoxU, and HoxY
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C461A
-
site-directed mutagenesis, catalytic subunit HoxH allele, mutant strain does not grow, inactive
D456N
-
site-directed mutagenesis, catalytic subunit HoxH allele, mutant strain does not grow, nearly inactive
D456S
-
site-directed mutagenesis, catalytic subunit HoxH allele, mutant strain does not grow, nearly inactive
E14Q
-
site-directed mutagenesis, catalytic subunit HoxH allele, mutant strain does not grow, inactive
E14V
-
site-directed mutagenesis, catalytic subunit HoxH allele, mutant strain does not grow, nearly inactive
G15A
-
site-directed mutagenesis, catalytic subunit HoxH allele, mutant strain does not grow, nearly inactive
H396L
-
site-directed mutagenesis, catalytic subunit HoxH allele, highly reduced activity compared to the wild-type strain
H396Q
-
site-directed mutagenesis, catalytic subunit HoxH allele, about 3.5fold reduced activity compared to the wild-type strain
H69Q
-
site-directed mutagenesis, catalytic subunit HoxH allele, about 5fold reduced activity compared to the wild-type strain
H69Q/P390A
-
site-directed mutagenesis, catalytic subunit HoxH alleles, reduced activity compared to the wild-type strain
I64A
-
site-directed mutagenesis, catalytic subunit HoxH allele, mutant strain does not grow, highly reduced activity compared to the wild-type strain
L118A
-
site-directed mutagenesis, catalytic subunit HoxH allele, reduced activity compared to the wild-type strain
L118F
-
site-directed mutagenesis, catalytic subunit HoxH allele, mutant strain does not grow at O2 concentrations above 5%, about 4fold reduced activity compared to the wild-type strain
L118I
-
site-directed mutagenesis, catalytic subunit HoxH allele, reduced activity compared to the wild-type strain
L394A
-
site-directed mutagenesis, catalytic subunit HoxH allele, about 5fold reduced activity compared to the wild-type strain
L394N
-
site-directed mutagenesis, catalytic subunit HoxH allele, mutant strain does not grow, nearly inactive
P390A
-
site-directed mutagenesis, catalytic subunit HoxH allele, about 5fold reduced activity compared to the wild-type strain
R12L
-
site-directed mutagenesis, catalytic subunit HoxH allele, mutant strain does not grow, highly reduced activity compared to the wild-type strain
R12Q
-
site-directed mutagenesis, catalytic subunit HoxH allele, mutant strain does not grow, highly reduced activity compared to the wild-type strain
R391L
-
site-directed mutagenesis, catalytic subunit HoxH allele, mutant strain does not grow, inactive
R391Q
-
site-directed mutagenesis, catalytic subunit HoxH allele, mutant strain does not grow, inactive
R60Q
-
site-directed mutagenesis, catalytic subunit HoxH allele, highly reduced activity compared to the wild-type strain
S68V
-
site-directed mutagenesis, catalytic subunit HoxH allele, highly reduced activity compared to the wild-type strain
T415S
-
site-directed mutagenesis, catalytic subunit HoxH allele, about 5fold reduced activity compared to the wild-type strain
T415V
-
site-directed mutagenesis, catalytic subunit HoxH allele, highly reduced activity compared to the wild-type strain
T415V/N415H
-
site-directed mutagenesis, catalytic subunit HoxH alleles, O2-sensitive growth, highly reduced activity compared to the wild-type strain
H16L

-
site-directed mutagenesis, catalytic subunit HoxH allele, mutant strain does not grow, highly reduced activity compared to the wild-type strain
H16L
-
in the HoxH-mutant protein H16L, H2 oxidation is impaired, but H2 production occurrs via a stable Ni-C state (N(III)-(H-)-Fe(II))
additional information

-
construction of an inactive null mutant strain, mutant strain growth characteristics, overview
additional information
-
construction of a HoxI deletion mutant enzyme, which shows different activation behaviour than the wild-type, it is not activated by and does not react with NADPH
additional information
-
construction of a HoxI deletion mutant enzyme, which shows different activation behaviour than the wild-type, it is not activated by and does not react with NADPH
-
additional information
in-frame deletion of HoxE, deletion of HoxH
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Burgdorf, T.; De Lacey, A.L.; Friedrich, B.
Functional analysis by site-directed mutagenesis of the NAD+-reducing hydrogenase from Ralstonia eutropha
J. Bacteriol.
184
6280-6288
2002
Cupriavidus necator
brenda
Tran-Betcke, A.; Warnecke, U.; Bƶcker, C.; Zaborosch, C.; Friedrich, B.
Cloning and nucleotide sequences of the genes for the subunits of NAD-reducing hydrogenase of Alcaligenes eutrophus H16
J. Bacteriol.
172
2920-2929
1990
Cupriavidus necator, Cupriavidus necator H16
brenda
Pfitzner, J.; Linke, H.A.B.; Schlegel, H.G.
Properties of the NAD-specific hydrogenase from Hydrogenomonas H 16
Arch. Mikrobiol.
71
67-78
1970
Hydrogenomonas sp., Hydrogenomonas sp. H16
brenda
Rohde, M.; Johannssen, W.; Mayer, F.
Immunocytochemical localization of the soluble NAD-dependent hydrogenase in cells of alcaligenes eutrophus
FEMS Microbiol. Lett.
36
83-86
1986
Cupriavidus necator
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brenda
Hyman, M.R.; Arp, D.J.
Reversible and irreversible effects of nitric oxide on the soluble hydrogenase from Alcaligenes eutrophus H16
Biochem. J.
254
469-475
1988
Cupriavidus necator, Cupriavidus necator H16
brenda
Hyman, M.R.; Fox, C.A.; Arp, D.J.
Role of hydrogen in the activation and regulation of hydrogen oxidation by the soluble hydrogenase from Alcaligenes eutrophus H16
Biochem. J.
254
463-468
1988
Cupriavidus necator
brenda
Popov, V.O.; Ovchinnikov, A.N.; Utkin, I.B.; Gazaryan, I.G.; Egorov, A.M.; Berezin, I.V.
Inactivation of the NAD-dependent hydrogenase from the hydrogen-oxidizing bacterium Alcaligenes eutrophus Z1: Thermoinactivation mechanism
Biochim. Biophys. Acta
831
297-301
1985
Cupriavidus necator, Cupriavidus necator Z1
-
brenda
Popov, V.O.; Gazaryan, I.G.; Egorov, A.M.; Berezin, I.V.
NAD-dependent hydrogenase from the hydrogen-oxidizing bacterium Alcaligenes eutrophum Z1. Kinetic studies of the NADH-dehydrogenase activity
Biochim. Biophys. Acta
827
466-471
1985
Cupriavidus necator, Cupriavidus necator Z1
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brenda
Schneider, K.; Schlegel, H.G.
Purification and properties of soluble hydrogenase from Alcaligenes eutrophus H 16
Biochim. Biophys. Acta
452
66-80
1976
Cupriavidus necator, Cupriavidus necator H16
brenda
Schneider, K.; Schlegel, H.G.
Localization and stability of hydrogenases from aerobic hydrogen bacteria
Arch. Microbiol.
112
229-238
1977
Cupriavidus necator, Cupriavidus necator b19, Cupriavidus necator G27, Cupriavidus necator H16, Cupriavidus necator N9A, no activity in Alcaligenes paradoxus, no activity in Aquaspirillum autotrophicum, no activity in Corynebacterium autotrophicum, no activity in Hydrogenophaga palleronii, no activity in Paracoccus denitrificans, no activity in Pseudomonas facilis
brenda
Aggag, M.; Schlegel, H.G.
Studies on a gram-positive hydrogen bacterium, Nocardia opaca 1 b. III. Purification, stability and some properties of the soluble hydrogen dehydrogenase
Arch. Microbiol.
100
25-39
1974
Rhodococcus opacus 1B, Rhodococcus opacus
brenda
Schneider, K.; Schlegel, H.G.; Jochim, K.
Effect of nickel on activity and subunit composition of purified hydrogenase from Nocardia opaca 1 b
Eur. J. Biochem.
138
553-541
1984
Rhodococcus opacus, Rhodococcus opacus 1B
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brenda
Schneider, K.; Cammack, R.; Schlegel, H.G.
Content and localization of FMN, Fe-S clusters and nickel in the NAD-linked hydrogenase of Nocardia opaca 1b
Eur. J. Biochem.
142
75-84
1984
Rhodococcus opacus 1B, Rhodococcus opacus
brenda
Petrov, R.R.; Utkin, I.B.; Popov, V.O.
Redox-dependent inactivation of the NAD-dependent hydrogenase from Alcaligenes eutrophus Z1
Arch. Biochem. Biophys.
268
298-305
1989
Cupriavidus necator, Cupriavidus necator Z1
brenda
Petrov, R.R.; Utkin, I.B.; Popov, V.O.
Effect of redox potential on the activation of the NAD-dependent hydrogenase from Alcaligenes eutrophus Z1
Arch. Biochem. Biophys.
268
287-297
1989
Cupriavidus necator, Cupriavidus necator Z1
brenda
Friedrich, C.G.; Suetin, S.; Lohmeyer, M.
Nickel and iron incoorporation into soluble hydrogenase of alcaligenes eutrophus
Arch. Microbiol.
140
206-211
1984
Cupriavidus necator, Cupriavidus necator H16
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brenda
Friedrich, C.G.; Schneider, K.; Friedrich, B.
Nickel in the catalytically active hydrogenase of Alcaligenes eutrophus
J. Bacteriol.
152
42-48
1982
Cupriavidus necator
brenda
Schneider, K.; Schlegel, H.G.
Production of superoxide radicals by soluble hydrogenase from Alcaligenes eutrophus H16
Biochem. J.
193
99-107
1981
Cupriavidus necator, Cupriavidus necator H16
brenda
Schneider, K.; Cammack, R.; Schlegel, H.G.; Hall, D.O.
The iron-sulphur centres of soluble hydrogenase from Alcaligenes eutrophus
Biochim. Biophys. Acta
578
445-461
1979
Cupriavidus necator
brenda
Schneider, K.; Schlegel, H.G.
Identification and quantitative determination of the flavin component of soluble hydrogenase from Alcaligenes eutrophus
Biochem. Biophys. Res. Commun.
84
564-571
1978
Cupriavidus necator
brenda
Grzeszik, C.; Ross, K.; Schneider, K.; Reh, M.; Schlegel, H.G.
Location, catalytic activity, and subunit composition of NAD-reducing hydrogenases of some Alcaligenes strains and Rhodococcus opacus MR22
Arch. Microbiol.
167
172-176
1997
Achromobacter denitrificans 4a-2, Achromobacter denitrificans, Achromobacter ruhlandii, Cupriavidus necator, Cupriavidus necator Cd2/01, Cupriavidus necator H16, Rhodococcus opacus
brenda
Happe, R.P.; Roseboom, W.; Egert, G.; Friedrich, C.G.; Massanz, C.; Friedrich, B.; Albracht, S.P.
Unusual FTIR and EPR properties of the H2-activating site of the cytoplasmic NAD-reducing hydrogenase from Ralstonia eutropha
FEBS Lett.
466
259-263
2000
Cupriavidus necator
brenda
Porthun, A.; Bernhard, M.; Friedrich, B.
Expression of a functional NAD-reducing [NiFe] hydrogenase from the gram-positive Rhodococcus opacus in the gram-negative Ralstonia eutropha
Arch. Microbiol.
177
159-166
2002
Rhodococcus opacus, Rhodococcus opacus MR11
brenda
Rakhely, G.; Kovacs, A.T.; Maroti, G.; Fodor, B.D.; Csanadi, G.; Latinovics, D.; Kovacs, K.L.
Cyanobacterial-type, heteropentameric, NAD+-reducing NiFe hydrogenase in the purple sulfur photosynthetic bacterium Thiocapsa roseopersicina
Appl. Environ. Microbiol.
70
722-728
2004
Thiocapsa roseopersicina (Q6XQK5), Thiocapsa roseopersicina
brenda
Hanczar, T.; Csaki, R.; Bodrossy, L.; Murrell, J.C.; Kovacs, K.L.
Detection and localization of two hydrogenases in Methylococcus capsulatus (Bath) and their potential role in methane metabolism
Arch. Microbiol.
177
167-172
2002
Methylococcus capsulatus
brenda
Loescher, S.; Burgdorf, T.; Buhrke, T.; Friedrich, B.; Dau, H.; Haumann, M.
Non-standard structures of the Ni-Fe cofactor in the regulatory and the NAD-reducing hydrogenases from Ralstonia eutropha
Biochem. Soc. Trans.
33
25-27
2005
Cupriavidus necator
brenda
Tikhonova, T.V.; Savel'eva, N.D.; Popov, V.O.
Chemical modification of catalytically essential functional groups of NAD-dependent hydrogenase from Ralstonia eutropha H16
Biochemistry
68
994-1001
2003
Cupriavidus necator, Cupriavidus necator H16
brenda
Schmitz, O.; Boison, G.; Salzmann, H.; Bothe, H.; Schutz, K.; Wang, S.H.; Happe, T.
HoxE - a subunit specific for the pentameric bidirectional hydrogenase complex (HoxEFUYH) of cyanobacteria
Biochim. Biophys. Acta
1554
66-74
2002
Synechocystis sp. (Q9Z354)
brenda
Leul, M.; Mohapatra, A.; Sellstedt, A.
Biodiversity of hydrogenases in Frankia
Curr. Microbiol.
50
17-23
2005
Frankia sp.
brenda
Mohapatra, A.; Leul, M.; Mattsson, U.; Sellstedt, A.
A hydrogen-evolving enzyme is present in Frankia sp. R43
FEMS Microbiol. Lett.
236
235-240
2004
Frankia sp. R43 (P22317), Frankia sp. R43 (P22318), Frankia sp. R43 (P22319), Frankia sp. R43 (P22320)
brenda
Burgdorf, T.; van der Linden, E.; Bernhard, M.; Yin, Q.Y.; Back, J.W.; Hartog, A.F.; Muijsers, A.O.; de Koster, C.G.; Albracht, S.P.; Friedrich, B.
The soluble NAD+-Reducing [NiFe]-hydrogenase from Ralstonia eutropha H16 consists of six subunits and can be specifically activated by NADPH
J. Bacteriol.
187
3122-3132
2005
Cupriavidus necator, Cupriavidus necator H16
brenda
Van der Linden, E.; Burgdorf, T.; Bernhard, M.; Bleijlevens, B.; Friedrich, B.; Albracht, S.P.
The soluble [NiFe]-hydrogenase from Ralstonia eutropha contains four cyanides in its active site, one of which is responsible for the insensitivity towards oxygen
J. Biol. Inorg. Chem.
9
616-626
2004
Cupriavidus necator
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
Loescher, S.; Burgdorf, T.; Zebger, I.; Hildebrandt, P.; Dau, H.; Friedrich, B.; Haumann, M.
Bias from H2 cleavage to production and coordination changes at the Ni-Fe active site in the NAD+-reducing hydrogenase from Ralstonia eutropha
Biochemistry
45
11658-11665
2006
Cupriavidus necator
brenda
Tikhonova, T.V.; Kurkin, S.A.; Klyachko, N.L.; Popov, V.O.
Use of a reverse micelle system for study of oligomeric structure of NAD+-reducing hydrogenase from Ralstonia eutropha H16
Biochemistry
70
645-651
2005
Cupriavidus necator, Cupriavidus necator H16
brenda
Serebryakova, L.T.; Sheremetieva, M.E.
Characterization of catalytic properties of hydrogenase isolated from the unicellular cyanobacterium Gloeocapsa alpicola CALU 743
Biochemistry
71
1370-1376
2006
Gloeocapsa alpicola, Gloeocapsa alpicola CALU 743
brenda
Vignais, P.M.
H/D exchange reactions and mechanistic aspects of the hydrogenases
Coord. Chem. Rev.
249
1677-1690
2005
Cupriavidus necator
-
brenda
Burgdorf, T.; Loescher, S.; Liebisch, P.; Van der Linden, E.; Galander, M.; Lendzian, F.; Meyer-Klaucke, W.; Albracht, S.P.; Friedrich, B.; Dau, H.; Haumann, M.
Structural and oxidation-state changes at its nonstandard Ni-Fe site during activation of the NAD-reducing hydrogenase from Ralstonia eutropha detected by X-ray absorption, EPR, and FTIR spectroscopy
J. Am. Chem. Soc.
127
576-592
2005
Cupriavidus necator
brenda
van der Linden, E.; Burgdorf, T.; de Lacey, A.L.; Buhrke, T.; Scholte, M.; Fernandez, V.M.; Friedrich, B.; Albracht, S.P.
An improved purification procedure for the soluble [NiFe]-hydrogenase of Ralstonia eutropha: new insights into its (in)stability and spectroscopic properties
J. Biol. Inorg. Chem.
11
247-260
2006
Cupriavidus necator, Cupriavidus necator H16
brenda
Burgdorf, T.; Lenz, O.; Buhrke, T.; van der Linden, E.; Jones, A.K.; Albracht, S.P.; Friedrich, B.
[NiFe]-hydrogenases of Ralstonia eutropha H16: modular enzymes for oxygen-tolerant biological hydrogen oxidation
J. Mol. Microbiol. Biotechnol.
10
181-196
2005
Cupriavidus necator, Cupriavidus necator H16
brenda
Arai, T.; Watanabe, S.; Matsumi, R.; Atomi, H.; Imanaka, T.; Miki, K.
Crystallization and preliminary X-ray crystallographic study of [NiFe]-hydrogenase maturation factor HypE from Thermococcus kodakaraensis KOD1
Acta Crystallogr. Sect. F
63
765-767
2007
Thermococcus kodakarensis
brenda
Kellers, P.; Ogata, H.; Lubitz, W.
Purification, crystallization and preliminary X-ray analysis of the membrane-bound [NiFe] hydrogenase from Allochromatium vinosum
Acta Crystallogr. Sect. F
64
719-722
2008
Allochromatium vinosum
brenda
Rakhely, G.; Laurinavichene, T.V.; Tsygankov, A.A.; Kovacs, K.L.
The role of Hox hydrogenase in the H2 metabolism of Thiocapsa roseopersicina
Biochim. Biophys. Acta
1767
671-676
2007
Thiocapsa roseopersicina, Thiocapsa roseopersicina Bbs
brenda
Oliveira, P.; Lindblad, P.
An AbrB-like protein regulates the expression of the bidirectional hydrogenase in Synechocystis sp. strain PCC 6803
J. Bacteriol.
190
1011-1019
2008
Synechocystis sp.
brenda
Rangarajan, E.S.; Asinas, A.; Proteau, A.; Munger, C.; Baardsnes, J.; Iannuzzi, P.; Matte, A.; Cygler, M.
Structure of [NiFe] hydrogenase maturation protein HypE from Escherichia coli and its interaction with HypF
J. Bacteriol.
190
1447-1458
2008
Escherichia coli
brenda
Watanabe, S.; Matsumi, R.; Arai, T.; Atomi, H.; Imanaka, T.; Miki, K.
Crystal structures of [NiFe] hydrogenase maturation proteins HypC, HypD, and HypE: insights into cyanation reaction by thiol redox signaling
Mol. Cell
27
29-40
2007
Thermococcus kodakarensis
brenda
Fdez Galvan, I.; Volbeda, A.; Fontecilla-Camps, J.C.; Field, M.J.
A QM/MM study of proton transport pathways in a [NiFe] hydrogenase
Proteins
73
195-203
2008
Desulfovibrio fructosivorans
brenda
Germer, F.; Zebger, I.; Saggu, M.; Lendzian, F.; Schulz, R.; Appel, J.
Overexpression, isolation and spectroscopic characterization of the bidirectional [NiFe]-hydrogenase from Synechocystis sp. PCC 6803
J. Biol. Chem.
284
36462-36472
2009
Synechocystis sp.
brenda
Kiss, E.; Kos, P.B.; Vass, I.
Transcriptional regulation of the bidirectional hydrogenase in the cyanobacterium Synechocystis 6803
J. Biotechnol.
142
31-37
2009
Synechocystis sp. PCC 6803
brenda
Ohki, Y.; Yasumura, K.; Kuge, K.; Tanino, S.; Ando, M.; Li, Z.; Tatsumi, K.
Thiolate-bridged dinuclear iron(tris-carbonyl)-nickel complexes relevant to the active site of [NiFe] hydrogenase
Proc. Natl. Acad. Sci. USA
105
7652-7657
2008
synthetic construct
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
Worm, P.; Stams, A.J.; Cheng, X.; Plugge, C.M.
Growth- and substrate-dependent transcription of formate dehydrogenase and hydrogenase coding genes in Syntrophobacter fumaroxidans and Methanospirillum hungatei
Microbiology
157
280-289
2011
Methanospirillum hungatei, Methanospirillum hungatei JF-1 (DSM 864), Syntrophobacter fumaroxidans, Syntrophobacter fumaroxidans MPOB (DSM 10017)
brenda
Ratzka, J.; Lauterbach, L.; Lenz, O.; Ansorge-Schumacher, M.
Systematic evaluation of the dihydrogen-oxidising and NAD +-reducing soluble [NiFe]-hydrogenase from Ralstonia eutropha H16 as a cofactor regeneration catalyst
Biocatal. Biotransform.
29
246-252
2011
Cupriavidus necator, Cupriavidus necator DSM 428
-
brenda
Lauterbach, L.; Liu, J.; Horch, M.; Hummel, P.; Schwarze, A.; Haumann, M.; Vincent, K.; Lenz, O.; Zebger, I.
The hydrogenase subcomplex of the NAD+-reducing [NiFe] hydrogenase from Ralstonia eutropha - Insights into catalysis and redox interconversions
Eur. J. Inorg. Chem.
2011
1067-1079
2011
Cupriavidus necator (P22319), Cupriavidus necator (P22320), Cupriavidus necator DSM 428 (P22319), Cupriavidus necator DSM 428 (P22320)
-
brenda
Herr, N.; Ratzka, J.; Lauterbach, L.; Lenz, O.; Ansorge-Schumacher, M.
Stability enhancement of an O2-tolerant NAD+-reducing [NiFe]-hydrogenase by a combination of immobilisation and chemical modification
J. Mol. Catal. B
97
169-174
2013
Cupriavidus necator, Cupriavidus necator DSM 428
-
brenda
Lauterbach, L.; Idris, Z.; Vincent, K.; Lenz, O.
Catalytic properties of the isolated diaphorase fragment of the NAD +-reducing [NiFe]-hydrogenase from Ralstonia eutropha
PLoS ONE
6
e25939
2011
Cupriavidus necator, Cupriavidus necator (P22317), Cupriavidus necator (P22318), Cupriavidus necator DSM 428 (P22317), Cupriavidus necator DSM 428 (P22318)
brenda
Schiffels, J.; Pinkenburg, O.; Schelden, M.; Aboulnaga, e.l.-.H.A.; Baumann, M.E.; Selmer, T.
An innovative cloning platform enables large-scale production and maturation of an oxygen-tolerant [NiFe]-hydrogenase from Cupriavidus necator in Escherichia coli
PLoS ONE
8
e68812
2013
Cupriavidus necator
brenda