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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
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+ + reduced methyl viologen
H2 + oxidized methyl viologen
-
-
-
-
?
H2
H+ + e-
-
hydrogenase reaction part
-
-
r
H2 + acceptor
H+ + reduced acceptor
-
-
-
-
?
H2 + ferricyanide
H+ + ferrocyanide
H2 + ferrocyanide
H+ + ferricyanide
-
-
-
-
r
H2 + oxidized benzyl viologen
H+ + reduced benzyl viologen
H2 + oxidized benzyl viologen
reduced benzyl viologen + H+
-
-
-
-
?
H2 + oxidized methyl viologen
H+ + reduced methyl viologen
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 + 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+
-
-
-
-
r
oxidized cytochrome c + NAD(P)H
reduced cytchrome c + NAD(P)+
-
-
-
?
oxidized methylene blue + NAD(P)H
reduced methylene blue + NAD(P)+
-
-
-
?
oxidized methylene blue + NADH + H+
reduced methylene blue + NAD+
-
-
-
-
r
oxidized resazurin + NADH + H+
reduced resazurin + NAD+
-
-
-
-
r
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+
-
-
-
?
ferrocyanide + NAD+
ferricyanide + NADH
-
-
-
-
r
ferrocyanide + NAD+
ferricyanide + NADH
-
diaphorase activity
-
-
r
H2 + ferricyanide
H+ + ferrocyanide
-
-
-
-
r
H2 + ferricyanide
H+ + ferrocyanide
-
708% activity compared to electron acceptor NAD+
-
?
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 + 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 methyl viologen
H+ + reduced methyl viologen
-
-
-
?
H2 + oxidized methyl viologen
H+ + reduced methyl viologen
-
-
-
r
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
-
-
?
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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 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 an inactive null mutant strain, mutant strain growth characteristics, overview
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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.; Bcker, 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 / ATCC 23440 / NCIB 10442 / S-10-1
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
-
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 / ATCC 23440 / NCIB 10442 / S-10-1
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
-
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 / ATCC 23440 / NCIB 10442 / S-10-1
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 / ATCC 23440 / NCIB 10442 / S-10-1, 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
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 / ATCC 23440 / NCIB 10442 / S-10-1
-
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 / ATCC 23440 / NCIB 10442 / S-10-1
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, Achromobacter denitrificans 4a-2, Achromobacter ruhlandii, Cupriavidus necator, Cupriavidus necator Cd2/01, Cupriavidus necator H16 / ATCC 23440 / NCIB 10442 / S-10-1, 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
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 / ATCC 23440 / NCIB 10442 / S-10-1
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 / ATCC 23440 / NCIB 10442 / S-10-1
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
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 / ATCC 23440 / NCIB 10442 / S-10-1
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 / ATCC 23440 / NCIB 10442 / S-10-1
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 / ATCC 23440 / NCIB 10442 / S-10-1
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
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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)
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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
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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 (P22317), Cupriavidus necator (P22318), Cupriavidus necator, 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
Puggioni, V.; Tempel, S.; Latifi, A.
Distribution of hydrogenases in Cyanobacteria a phylum-wide genomic survey
Front. Genet.
7
223
2016
Cupriavidus necator (P22319), Cupriavidus necator ATCC 17699 (P22319)
brenda