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Information on EC 1.12.98.4 - sulfhydrogenase and Organism(s) Pyrococcus furiosus and UniProt Accession Q8U2E5
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1.12.98.4 sulfhydrogenaseIUBMB Comments
An iron-sulfur protein. The enzyme from the hyperthermophilic archaeon Pyrococcus furiosus is part of two heterotetrameric complexes where the beta and gamma subunits function as sulfur reductase and the alpha and delta subunits function as hydrogenases (EC 1.12.1.3, hydrogen dehydrogenase [NADP+] and EC 1.12.1.4, hydrogen dehydrogenase [NAD(P)+], respectively). Sulfur can also be used as substrate, but since it is insoluble in aqueous solution and polysulfide is generated abiotically by the reaction of hydrogen sulfide and sulfur, polysulfide is believed to be the true substrate .
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Word Map
- 1.12.98.4
- h2s
- hydrogenases
- succinogenes
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wolinella
- pasteurianum
-
sulfur-reducing
- tetrathionate
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chemolithotrophic
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sulfur-dependent
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molybdoenzyme
- energy production
The taxonomic range for the selected organisms is: Pyrococcus furiosus
The expected taxonomic range for this enzyme is: Archaea, Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Archaea, Bacteria, Eukaryota
Synonyms
hydrogenase ii, sulfur reductase, polysulfide reductase, sulfhydrogenase, polysulfide dehydrogenase, sulhydrogenase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
H2:sulfuroxidoreductase complex
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reductase, sulfur
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sulfhydrogenase
sulfhydrogenase
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bifunctional enzyme using both elementar sulfur and polysulfide as substrates for H2S production
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY SOURCE
PATHWAYS
BRENDA
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-, -
SYSTEMATIC NAME
IUBMB Comments
H2:polysulfide oxidoreductase
An iron-sulfur protein. The enzyme from the hyperthermophilic archaeon Pyrococcus furiosus is part of two heterotetrameric complexes where the beta and gamma subunits function as sulfur reductase and the alpha and delta subunits function as hydrogenases (EC 1.12.1.3, hydrogen dehydrogenase [NADP+] and EC 1.12.1.4, hydrogen dehydrogenase [NAD(P)+], respectively). Sulfur can also be used as substrate, but since it is insoluble in aqueous solution and polysulfide is generated abiotically by the reaction of hydrogen sulfide and sulfur, polysulfide is believed to be the true substrate [2].
CAS REGISTRY NUMBER
COMMENTARY
101637-43-8
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
H2 + benzyl viologen
H2S + reduced benzyl viologen
highest activity
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-
?
H2S + NADH + H+
H2 + NAD+
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NADH is a very inefficient electron carrier for sulfhydrogenase
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r
NADPH + H+ + polysulfide(n)
NADP+ + polysulfide(n-1)
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r
H2 + methyl viologen
H2S + reduced methyl viologen
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?
H2 + polysulfide(n)
H2S + polysulfide(n-1)
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r
additional information
?
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ferredoxin from Pyrococcus furiosus is not an efficient electron carrier
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?
additional information
?
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ferredoxin from Pyrococcus furiosus is not an efficient electron carrier
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?
additional information
?
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ferredoxin is not an effective electron donor for Pyrococcus furiosus sulfhydrogenase. NAD+ is not reduced
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
NADPH and NADH are equally efficient as electron donors for H2 production
NADPH
NADPH and NADH are equally efficient as electron donors for H2 production
[Ni-Fe]-center
the alpha-subunit carries the NiFe dinuclear center
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FAD
the gamma-subunit contains one FAD molecule
[2Fe-2S]-center
contains 1 [2Fe-2S] center
[2Fe-2S]-center
the gamma-subunit contains one 2Fe-2S cluster
[4Fe-4S]-center
contains 2 [4Fe-4S]-centers
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
contains 21 atoms iron per mol enzyme
Iron
the alpha-subunit carries the NiFe dinuclear center
Ni2+
Nickel
the alpha-subunit carries the NiFe dinuclear center
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
E7FI44: alpha-subunit, Q8U2E5: beta-subunit, Q8U2E4: gamma-subunit, E7FHU4: delta-subunit
SwissProt
E7FI44: subunit alpha, Q8U2E5: subunit beta, E7FHU4: subunit delta, Q8U2E4: subunit gamma. Heterotetrameric complex where the alpha and delta subunits function as a hydrogenase (EC 1.12.1.3) while the beta and gamma subunits function as sulfur reductase
SwissProt
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
24000
1 * 52000 + 1 * 39000 + 1 * 30000 + 1 * 24000, SDS-PAGE
30000
1 * 52000 + 1 * 39000 + 1 * 30000 + 1 * 24000, SDS-PAGE
39000
1 * 52000 + 1 * 39000 + 1 * 30000 + 1 * 24000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterotetramer
tetramer
heterotetrameric complex where the alpha and delta subunits function as a hydrogenase (EC 1.12.1.3) while the beta and gamma subunits function as sulfur reductase
heterotetramer
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four subunits, alpha: 45000, beta: 43000, gamma: 31000, delta: 28000, SDS-PAGE
heterotetramer
1 * 52000 + 1 * 39000 + 1 * 30000 + 1 * 24000, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE column chromatography, hydroxyapatite column chromatography, phenyl Sepharose column chromatography, and Superdex 200 gel filtration
Q Sepharose column chromatography, hydroxyapatite column chromatography, and Mono Q column chromatography
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is repressed by SurR an archaeal transcriptional regulator and a key regulator involved in primary sulfur response
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
energy production
development of economically feasible production system for hydrogen as an alternative energy source of the future. The not-mediated Pyrococcus furiosus sulfhydrogenase/TiO2 system represents a first optimization step towards the development of an economically feasible in vitro hydrogen production process which should be driven by solar light and should utilize waste compounds as source of electrons
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Arendsen, A.F.; Veenhuizen, P.T.M.; Hagen, W.R.
Redox properties of the sulfhydrogenase from Pyrococcus furiosus
FEBS Lett.
368
117-121
1995
Pyrococcus furiosus
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 (E7FHC4 and E7FHN9 and E7FHW8 and E7FHF8), Pyrococcus furiosus
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
Yang, H.; Lipscomb, G.L.; Keese, A.M.; Schut, G.J.; Thomm, M.; Adams, M.W.; Wang, B.C.; Scott, R.A.
SurR regulates hydrogen production in Pyrococcus furiosus by a sulfur-dependent redox switch
Mol. Microbiol.
77
1111-1122
2010
Pyrococcus furiosus
Ma, K.; Hao, Z.; Adams, M.
Hydrogen production from pyruvate by enzymes purified from the hyperthermophilic archaeon, Pyrococcus furiosus: A key role for NADPH
FEMS Microbiol. Lett.
122
245-250
1994
Pyrococcus furiosus
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Pedroni, P.; Della Volpe, A.; Galli, G.; Mura, G.M.; Pratesi, C.; Grandi, G.
Characterization of the locus encoding the [Ni-Fe] sulfhydrogenase from the archaeon Pyrococcus furiosus: evidence for a relationship to bacterial sulfite reductases
Microbiology
141
449-458
1995
Pyrococcus furiosus (E7FI44 and Q8U2E5 and E7FHU4 and Q8U2E4), Pyrococcus furiosus
Silva, P.; De Castro, B.; Hagen, W.
On the prosthetic groups of the NiFe sulfhydrogenase from Pyrococcus furiosus Topology, structure, and temperature-dependent redox chemistry
J. Biol. Inorg. Chem.
4
284-291
1999
Pyrococcus furiosus (E7FI44 AND Q8U2E5 AND Q8U2E4 AND E7FHU4), Pyrococcus furiosus
Selvaggi, A.; Tosi, C.; Barberini, U.; Franchi, E.; Rodriguez, F.; Pedroni, P.
In vitro hydrogen photoproduction using Pyrococcus furiosus sulfhydrogenase and TiO2
J. Photochem. Photobiol. A
125
107-112
1999
Pyrococcus furiosus (E7FI44 AND Q8U2E5 AND Q8U2E4 AND E7FHU4)
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