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Information on EC 1.12.7.2 - ferredoxin hydrogenase and Organism(s) Pyrococcus furiosus and UniProt Accession Q8U0Z6

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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.
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This record set is specific for:
Pyrococcus furiosus
UNIPROT: Q8U0Z6
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Word Map
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, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MbhL
membrane-bound hydrogenase subunit alpha
bidirectional hydrogenase
-
-
-
-
C-MBH
engineered minimal catalytically active 4-subunit subcomplex of respiratory membrane-bound hydrogenase
Fe hydrogenlyase
-
-
-
-
H2 oxidizing hydrogenase
-
-
-
-
H2 producing hydrogenase [ambiguous]
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-
-
-
HYD1
-
-
-
-
HYD2
-
-
-
-
hydrogen-lyase [ambiguous]
-
-
-
-
hydrogenase (ferredoxin)
-
-
-
-
hydrogenase I
-
-
-
-
hydrogenase II
-
-
-
-
hydrogenlyase
-
-
-
-
hydrogenlyase [ambiguous]
-
-
-
-
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
-
-
membrane-bound hydrogenase
-
-
NiFe hydrogenase
-
-
-
-
uptake hydrogenase [ambiguous]
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
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.
CAS REGISTRY NUMBER
COMMENTARY hide
9080-02-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
H+ + NADH
H2 + NAD+
show the reaction diagram
-
-
-
-
r
H+ + reduced ferredoxin
H2 + oxidized ferredoxin
show the reaction diagram
H+ + reduced methyl viologen
H2 + oxidized methyl viologen
show the reaction diagram
-
-
-
-
?
H2 + 2 oxidized ferredoxin
2 reduced ferredoxin + 2 H+
show the reaction diagram
-
-
-
?
H2 + electron acceptor
H+ + reduced electron acceptor
show the reaction diagram
H2 + methyl viologen
reduced methyl viologen + H+
show the reaction diagram
-
-
-
-
?
H2 + NAD+
H+ + NADH
show the reaction diagram
-
-
-
-
r
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
-
-
-
r
H2 + oxidized ferredoxin
reduced ferredoxin + H+
show the reaction diagram
-
-
-
-
?
S + NADPH
H2S + NADP+
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
H+ + reduced ferredoxin
H2 + oxidized ferredoxin
show the reaction diagram
H2 + oxidized ferredoxin
H+ + reduced ferredoxin
show the reaction diagram
-
-
-
r
H2 + oxidized ferredoxin
reduced ferredoxin + H+
show the reaction diagram
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
-
putative nucleotide-binding site in the gamma subunit
NADPH
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
rubredoxin
-
3fold increase of sulfur reductase activity at pH 7.6
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1
methyl viologen
-
at 120 kPa H2
0.125
NAD+
-
-
0.07
NADH
-
-
0.017
NADP+
-
-
0.07
NADPH
-
-
1.25
reduced methyl viologen
-
-
0.2
sulfur
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.004
-
hydrogen oxidation, benzyl viologen as electron acceptor
0.02
-
hydrogen production, oxidized ferredoxin as electron donor, hydrogenase II
0.2
-
sulfur reduction, hydrogenase II
0.98
-
hydrogen production, sodium dithionite as electron donor, hydrogenase II
11
-
hydrogen oxidation, methyl viologen as electron acceptor, hydrogenase II
131
-
hydrogen oxidation, benzyl viologen as electron acceptor, hydrogenase II
40
-
hydrogen production, methyl viologen as electron donor, hydrogenase II
9.4
-
hydrogen evolution, reduced methyl viologen as electron donor
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8
-
hydrogen oxidation
8.4
-
sulfur reductase activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
the minimal catalytically active 4-subunit subcomplex of respiratory membrane-bound hydrogenase, H2 formation with the physiological electron donor, reduced ferredoxin
80
-
sulfur reductase activity
90
-
above 90°C, hydrogenase II
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.6
calculated from sequence
5
calculated from sequence
6
calculated from sequence
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
enzyme of hydrogen metabolism
physiological function
enzyme of hydrogen metabolism
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
47934
x * 47934, calculated from sequence
18284
x * 18284, calculated from sequence
185000
-
gel filtration
20000
-
alpha, beta, 1 * 40000 + 1 * 20000, SDS-PAGE
20184
x * 20184, calculated from sequence
24000
27000
-
alpha, beta, gamma, 2 * 46000 + 2 * 27000 + 2 * 24000, SDS-PAGE
30000
-
alpha, beta, gamma, delta, 2 * 52000 + 2 * 39000 + 2 * 30000 + 2 * 24000, SDS-PAGE
310000
-
gel filtration
320000
-
gel filtration
39000
-
alpha, beta, gamma, delta, 2 * 52000 + 2 * 39000 + 2 * 30000 + 2 * 24000, SDS-PAGE
40000
-
alpha, beta, 1 * 40000 + 1 * 20000, SDS-PAGE
46000
-
alpha, beta, gamma, 2 * 46000 + 2 * 27000 + 2 * 24000, SDS-PAGE
52000
-
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 47934, calculated from sequence
dimer
-
alpha, beta, 1 * 40000 + 1 * 20000, SDS-PAGE
hexamer
-
alpha, beta, gamma, 2 * 46000 + 2 * 27000 + 2 * 24000, SDS-PAGE
octamer
-
alpha, beta, gamma, delta, 2 * 52000 + 2 * 39000 + 2 * 30000 + 2 * 24000, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
95
-
50% inactivation after 6 h, hydrogenase II
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
rapid inactivation under aerobic conditions
-
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA column chromatography
-
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
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team