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IUBMB Comments Contains iron-sulfur clusters. The enzymes from some sources contains nickel. Can use molecular hydrogen for the reduction of a variety of substances.
The taxonomic range for the selected organisms is: Pyrococcus furiosus The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
membrane-bound hydrogenase, hydrogenase i, bidirectional hydrogenase, hydrogenlyase, fe-fe hydrogenase, [fefe] hydrogenase hyda1, c-mbh, ddhydab, ferredoxin-dependent [fefe]-hydrogenase, mbh hydrogenase,
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MbhL
membrane-bound hydrogenase subunit alpha
bidirectional hydrogenase
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C-MBH
engineered minimal catalytically active 4-subunit subcomplex of respiratory membrane-bound hydrogenase
H2 oxidizing hydrogenase
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H2 producing hydrogenase [ambiguous]
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hydrogen-lyase [ambiguous]
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hydrogenase (ferredoxin)
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hydrogenlyase [ambiguous]
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MbhJ
subunit of membrane-bound hydrogenase
MbhJKLN
engineered minimal catalytically active 4-subunit subcomplex of respiratory membrane-bound hydrogenase, MbhJKLN
MbhK
membrane-bound hydrogenase subunit beta
membrane bound NiFe hydrogenase
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membrane-bound hydrogenase
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uptake hydrogenase [ambiguous]
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-
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hydrogen:ferredoxin oxidoreductase
Contains iron-sulfur clusters. The enzymes from some sources contains nickel. Can use molecular hydrogen for the reduction of a variety of substances.
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H+ + NADH
H2 + NAD+
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-
-
-
r
H+ + reduced ferredoxin
H2 + oxidized ferredoxin
H+ + reduced methyl viologen
H2 + oxidized methyl viologen
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-
-
-
?
H2 + 2 oxidized ferredoxin
2 reduced ferredoxin + 2 H+
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-
-
?
H2 + electron acceptor
H+ + reduced electron acceptor
H2 + methyl viologen
reduced methyl viologen + H+
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-
-
-
?
H2 + NAD+
H+ + NADH
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-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
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-
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r
H2 + oxidized ferredoxin
reduced ferredoxin + H+
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-
-
-
?
additional information
?
-
H+ + reduced ferredoxin
H2 + oxidized ferredoxin
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-
-
-
?
H+ + reduced ferredoxin
H2 + oxidized ferredoxin
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Mbh function as a redox-driven ion pump coupling the reduction of protons with electrons derived from the oxidation of a low-potential ferredoxin to the generation of a H+ motive force
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-
?
H+ + reduced ferredoxin
H2 + oxidized ferredoxin
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the exergonic reaction is coupled to energy conservation by means of electron-transport phosphorylation
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-
?
H2 + electron acceptor
H+ + reduced electron acceptor
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methylene blue as electron acceptor
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-
r
H2 + electron acceptor
H+ + reduced electron acceptor
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methyl viologen as electron acceptor
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-
r
H2 + electron acceptor
H+ + reduced electron acceptor
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benzyl viologen as electron acceptor
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r
H2 + electron acceptor
H+ + reduced electron acceptor
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NADP+ as electron acceptor
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-
r
S + NADPH
H2S + NADP+
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-
-
?
S + NADPH
H2S + NADP+
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-
-
-
?
additional information
?
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ferredoxin is not an efficient electron carrier for both hydrogenases
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-
?
additional information
?
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ferredoxin is not an efficient electron carrier for both hydrogenases
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-
?
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H+ + reduced ferredoxin
H2 + oxidized ferredoxin
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
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-
-
r
H2 + oxidized ferredoxin
reduced ferredoxin + H+
-
-
-
-
?
H+ + reduced ferredoxin
H2 + oxidized ferredoxin
-
Mbh function as a redox-driven ion pump coupling the reduction of protons with electrons derived from the oxidation of a low-potential ferredoxin to the generation of a H+ motive force
-
-
?
H+ + reduced ferredoxin
H2 + oxidized ferredoxin
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the exergonic reaction is coupled to energy conservation by means of electron-transport phosphorylation
-
-
?
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NADH
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putative nucleotide-binding site in the gamma subunit
FAD
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putative nucleotide-binding site in the gamma subunit
FAD
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hydrogenase II, 0.83 mol per mol heterotetramer
NADPH
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NADPH
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putative nucleotide-binding site in the gamma subunit
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Fe
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31 atoms per mol
Fe
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five [4Fe4S] clusters, 2 in the beta subunit and 3 in the delta subunit, additionally one [2Fe2S] cluster in the gamma subunit
Fe
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21 atoms per mol heterotetramer
Fe
-
4 Fe-atoms per mol hydrogenase
Fe
contains [NiFe]-clusters. The Fe: Ni ratio of the engineered and expressed His-tagged 4-subunit subcomplex of respiratory membrane-bound hydrogenase. Subunit MbhL harbors the [NiFe] active site, subunit MbhK is part of the large subunit, subunit MbhJ harbors one [4Fe4S] cluster and MbhN harbors two [4Fe4S] clusters
Ni
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0.98 atoms per mol enzyme
Ni
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1 Ni atom per mol, redox active Ni-site
Ni
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0.9 atoms per mol heterotetramer, NiFe-catalytic site in the alpha-subunit
Ni
contains [NiFe]-clusters. The Fe: Ni ratio of the engineered and expressed His-tagged 4-subunit subcomplex of respiratory membrane-bound hydrogenase. Subunit MbhL harbors the [NiFe] active site, subunit MbhK is part of the large subunit, subunit MbhJ harbors one [4Fe4S] cluster and MbhN harbors two [4Fe4S] clusters
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O2
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reversible inhibition
O2
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50% loss of H2 evolution activity after 3 h
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rubredoxin
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3fold increase of sulfur reductase activity at pH 7.6
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additional information
the enzyme is activated by an incubation of 20 min at 80°C under a hydrogen atmosphere
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additional information
the enzyme is activated by an incubation of 20 min at 80°C under a hydrogen atmosphere
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additional information
the enzyme is activated by an incubation of 20 min at 80°C under a hydrogen atmosphere
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additional information
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the enzyme is activated by an incubation of 20 min at 80°C under a hydrogen atmosphere
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1
methyl viologen
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at 120 kPa H2
1.25
reduced methyl viologen
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-
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0.004
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hydrogen oxidation, benzyl viologen as electron acceptor
0.02
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hydrogen production, oxidized ferredoxin as electron donor, hydrogenase II
0.2
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sulfur reduction, hydrogenase II
0.98
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hydrogen production, sodium dithionite as electron donor, hydrogenase II
11
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hydrogen oxidation, methyl viologen as electron acceptor, hydrogenase II
131
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hydrogen oxidation, benzyl viologen as electron acceptor, hydrogenase II
40
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hydrogen production, methyl viologen as electron donor, hydrogenase II
9.4
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hydrogen evolution, reduced methyl viologen as electron donor
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8.4
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sulfur reductase activity
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60
the minimal catalytically active 4-subunit subcomplex of respiratory membrane-bound hydrogenase, H2 formation with the physiological electron donor, reduced ferredoxin
80
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sulfur reductase activity
90
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above 90°C, hydrogenase II
95
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hydrogen evolution
95
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above 95°C, hydrogen oxidation
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6.6
calculated from sequence
5
calculated from sequence
6
calculated from sequence
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SwissProt
brenda
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brenda
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brenda
minimal catalytically active 4-subunit subcomplex of respiratory membrane-bound hydrogenase
brenda
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brenda
native 14-subunit membrane-bound subcomplex of respiratory membrane-bound hydrogenase
brenda
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physiological function
enzyme of hydrogen metabolism
physiological function
enzyme of hydrogen metabolism
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47934
x * 47934, calculated from sequence
18284
x * 18284, calculated from sequence
20000
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alpha, beta, 1 * 40000 + 1 * 20000, SDS-PAGE
20184
x * 20184, calculated from sequence
27000
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alpha, beta, gamma, 2 * 46000 + 2 * 27000 + 2 * 24000, SDS-PAGE
30000
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alpha, beta, gamma, delta, 2 * 52000 + 2 * 39000 + 2 * 30000 + 2 * 24000, SDS-PAGE
39000
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alpha, beta, gamma, delta, 2 * 52000 + 2 * 39000 + 2 * 30000 + 2 * 24000, SDS-PAGE
40000
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alpha, beta, 1 * 40000 + 1 * 20000, SDS-PAGE
46000
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alpha, beta, gamma, 2 * 46000 + 2 * 27000 + 2 * 24000, SDS-PAGE
52000
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alpha, beta, gamma, delta, 2 * 52000 + 2 * 39000 + 2 * 30000 + 2 * 24000, SDS-PAGE
85000
gel filtration, engineered minimal catalytically active 4-subunit subcomplex of respiratory membrane-bound hydrogenase
24000
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alpha, beta, gamma, delta, 2 * 52000 + 2 * 39000 + 2 * 30000 + 2 * 24000, SDS-PAGE
24000
-
alpha, beta, gamma, 2 * 46000 + 2 * 27000 + 2 * 24000, SDS-PAGE
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?
x * 47934, calculated from sequence
dimer
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alpha, beta, 1 * 40000 + 1 * 20000, SDS-PAGE
hexamer
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alpha, beta, gamma, 2 * 46000 + 2 * 27000 + 2 * 24000, SDS-PAGE
octamer
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alpha, beta, gamma, delta, 2 * 52000 + 2 * 39000 + 2 * 30000 + 2 * 24000, SDS-PAGE
?
x * 18284, calculated from sequence
?
x * 20184, calculated from sequence
?
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x * 298000, calculated from amino acid sequence
?
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x * 310000, small angle X-ray scattering
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additional information
engineering and expressing of a His-tagged minimal catalytically active 4-subunit cytoplasmic subcomplex of respiratory membrane-bound hydrogenase. In order to obtain a minimal subcomplex, the native MBH operon is splitt it into two separate transcriptional units
additional information
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engineering and expressing of a His-tagged minimal catalytically active 4-subunit cytoplasmic subcomplex of respiratory membrane-bound hydrogenase. In order to obtain a minimal subcomplex, the native MBH operon is splitt it into two separate transcriptional units
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95
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50% inactivation after 6 h, hydrogenase II
100
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50% inactivation after 30 min
100
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most of activity is retained after 1 h incubation
90
half-life of minimal catalytically active 4-subunit subcomplex of respiratory membrane-bound hydrogenase: 8 h. Half-life of the native 14-subunit membrane-bound respiratory membrane-bound hydrogenase complex
90
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the membrane-bound and purified enzymes show half-lives at 90°C of 1 and 25 h, respectively
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rapid inactivation under aerobic conditions
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439652
the O2 sensitivities of minimal catalytically active 4-subunit subcomplex of respiratory membrane-bound hydrogenase and the native 14-subunit membrane-bound version are similar, half-lives of about 15 h in air
730867
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Ni-NTA column chromatography
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purification of the engineered and expressed His-tagged 4-subunit cytoplasmic subcomplex of respiratory membrane-bound hydrogenase
under anaerobic conditions, solubilized with n-dodecyl-beta-D-maltoside
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Bryant, F.O.; Adams, M.W.W.
Characterization of hydrogenase from the hyperthermophilic archaebacterium, Pyrococcus furiosus
J. Biol. Chem.
264
5070-5079
1989
Pyrococcus furiosus
brenda
Ma, K.; Weiss, R.; Adams, M.W.W.
Characterization of hydrogenase II from the hyperthermophilic archaeon Pyrococcus furiosus and assessment of its role in sulfur reduction
J. Bacteriol.
182
1864-1871
2000
Pyrococcus furiosus
brenda
Sapra, R.; Verhagen, M.F.; Adams, M.W.
Purification and characterization of a membrane-bound hydrogenase from the hyperthermophilic archaeon Pyrococcus furiosus
J. Bacteriol.
182
3423-3428
2000
Pyrococcus furiosus
brenda
Ma, K.; Schicho, R.N.; Kelly, R.M.; Adams, M.W.W.
Hydrogenase of the hyperthermophile Pyrococcus furiosus is an elemental sulfur reductase or sulfhydrogenase: Evidence for a sulfur-reducing hydrogenase ancestor
Proc. Natl. Acad. Sci. USA
90
5341-5344
1993
Pyrococcus furiosus
brenda
Hedderich, R.
Energy-converting [NiFe] hydrogenases from archaea and extremophiles: ancestors of complex I
J. Bioenerg. Biomembr.
36
65-75
2004
Methanosarcina barkeri, Pyrococcus furiosus, Caldanaerobacter subterraneus subsp. tengcongensis
brenda
Hedderich, R.; Forzi, L.
Energy-converting [NiFe] hydrogenases: more than just H2 activation
J. Mol. Microbiol. Biotechnol.
10
92-104
2005
Carboxydothermus hydrogenoformans, Escherichia coli, Methanosarcina barkeri, Pyrococcus furiosus, Rhodospirillum rubrum, Caldanaerobacter subterraneus subsp. tengcongensis
brenda
Silva, P.J.; van den Ban, E.C.; Wassink, H.; Haaker, H.; de Castro, B.; Robb, F.T.; Hagen, W.R.
Enzymes of hydrogen metabolism in Pyrococcus furiosus
Eur. J. Biochem.
267
6541-6551
2000
Pyrococcus furiosus (Q8U0Z6), Pyrococcus furiosus (Q8U0Z7), Pyrococcus furiosus (Q8U0Z8), Pyrococcus furiosus
brenda
McTernan, P.M.; Chandrayan, S.K.; Wu, C.H.; Vaccaro, B.J.; Lancaster, W.A.; Adams, M.W.
Engineering the respiratory membrane-bound hydrogenase of the hyperthermophilic archaeon Pyrococcus furiosus and characterization of the catalytically active cytoplasmic subcomplex
Protein Eng. Des. Sel.
28
1-8
2015
Pyrococcus furiosus (Q8U0Z8 and Q8U0Z7 and Q8U0Z6), Pyrococcus furiosus
brenda
McTernan, P.M.; Chandrayan, S.K.; Wu, C.H.; Vaccaro, B.J.; Lancaster, W.A.; Yang, Q.; Fu, D.; Hura, G.L.; Tainer, J.A.; Adams, M.W.
Intact functional fourteen-subunit respiratory membrane-bound [NiFe]-hydrogenase complex of the hyperthermophilic archaeon Pyrococcus furiosus
J. Biol. Chem.
289
19364-19372
2014
Pyrococcus furiosus, Pyrococcus furiosus COM1
brenda
Transporter Classification Database (TCDB):
3.D.1.4.1