Biology:Cytochrome-c3 hydrogenase
| cytochrome-c3 hydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.12.2.1 | ||||||||
| CAS number | 9027-05-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a cytochrome-c3 hydrogenase (EC 1.12.2.1) is an enzyme that catalyzes the chemical reaction
- 2 H2 + ferricytochrome c3 [math]\displaystyle{ \rightleftharpoons }[/math] 4 H+ + ferrocytochrome c3
Thus, the two substrates of this enzyme are H2 and ferricytochrome c3, whereas its two products are H+ and ferrocytochrome c3.
This enzyme belongs to the family of oxidoreductases, specifically those acting on hydrogen as donor with a cytochrome as acceptor. The systematic name of this enzyme class is hydrogen:ferricytochrome-c3 oxidoreductase. Other names in common use include H2:ferricytochrome c3 oxidoreductase, cytochrome c3 reductase, cytochrome hydrogenase, and hydrogenase [ambiguous]. It has 3 cofactors: iron, Nickel, and Iron-sulfur.
Structural studies
As of late 2007, 19 structures have been solved for this class of enzymes, with PDB accession codes 1FRV, 1H2R, 1UBH, 1UBJ, 1UBK, 1UBL, 1UBM, 1UBO, 1UBR, 1UBT, 1UBU, 1WUH, 1WUI, 1WUJ, 1WUK, 1WUL, 1YQ9, 1YQW, and 1YRQ.
References
- DerVartanian DV; Le Gall J (1974). "A monomolecular electron transfer chain: structure and function of cytochrome c3". Biochim. Biophys. Acta 346 (1): 79–99. doi:10.1016/0304-4173(74)90012-3. PMID 4364940.
- "Single crystals of hydrogenase from Desulfovibrio vulgaris Miyazaki F". J. Biol. Chem. 262 (6): 2823–5. 1987. PMID 3546297.
- Rilkis E; Rittenberg D (1961). "Some observations on the enzyme, hydrogenase". J. Biol. Chem. 236: 2526–2529. PMID 13741672.
- Sadana JC; Morey AV (1961). "Purification and properties of the hydrogenase of Desulfovibrio desulfuricans". Biochim. Biophys. Acta 50: 153–163. doi:10.1016/0006-3002(61)91072-1. PMID 13745271.
- Fontecilla-Camps JC; Charon, MH; Piras, C; Hatchikian, EC; Frey, M; Fontecilla-Camps, JC (1995). "Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas". Nature 373 (6515): 580–7. doi:10.1038/373580a0. PMID 7854413. Bibcode: 1995Natur.373..580V.
- Fontecilla-Camps JC; Vernede, X; Hatchikian, EC; Volbeda, A; Frey, M; Fontecilla-Camps, JC (1999). "The crystal structure of a reduced [NiFeSe] hydrogenase provides an image of the activated catalytic center". Structure 7 (5): 557–66. doi:10.1016/S0969-2126(99)80072-0. PMID 10378275.
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