Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2 ferricyanide + NAD(P)H
2 ferrocyanide + NAD(P)+ + H+
FAD + H2
FADH2
-
99% activity compared to NAD+
-
-
r
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 + methyl viologen
-
-
-
-
?
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 2,6-dichlorophenol indophenol + NADH + H+
reduced 2,6-dichlorophenolindophenol + NAD+
oxidized benzyl viologen + NADH
reduced benzyl viologen + NAD+
oxidized cytochrome c + NAD(P)H
reduced cytchrome c + NAD(P)+
-
-
-
?
oxidized methylene blue + H2
reduced methylene blue + H+
-
1058% activity compared to NAD+
-
-
r
oxidized methylene blue + NAD(P)H
reduced methylene blue + NAD(P)+
-
-
-
?
oxidized methylene blue + NADH + H+
reduced methylene blue + NAD+
oxidized resazurin + NADH + H+
reduced resazurin + NAD+
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
-
-
-
-
?
H2 + NAD+
H+ + NADH
-
-
-
-
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
-
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
-
-
-
?
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
-
-
-
-
?
H2 + NAD+
H+ + NADH
-
-
-
r
H2 + NAD+
H+ + NADH
-
-
-
-
?
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
-
-
-
-
?
H2 + oxidized methyl viologen
H+ + reduced methyl viologen
-
-
-
-
?
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 2,6-dichlorophenol indophenol + NADH + H+
reduced 2,6-dichlorophenolindophenol + NAD+
-
-
-
-
r
oxidized 2,6-dichlorophenol indophenol + NADH + H+
reduced 2,6-dichlorophenolindophenol + NAD+
-
-
-
-
r
oxidized benzyl viologen + NADH
reduced benzyl viologen + NAD+
-
-
-
?
oxidized benzyl viologen + NADH
reduced benzyl viologen + NAD+
-
-
-
?
oxidized methylene blue + NADH + H+
reduced methylene blue + NAD+
-
-
-
-
r
oxidized methylene blue + NADH + H+
reduced methylene blue + NAD+
-
-
-
-
r
oxidized resazurin + NADH + H+
reduced resazurin + NAD+
-
-
-
-
r
oxidized resazurin + NADH + H+
reduced resazurin + NAD+
-
-
-
-
r
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
?
-
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
-
-
?
additional information
?
-
-
flavodoxin and ferredoxin directly reduce the enzyme in vitro
-
-
?