Cytochrome-c3 hydrogenase
| cytochrome-c3 hydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.12.2.1 | ||||||||
| CAS no. | 9027-05-8 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a cytochrome-c3 hydrogenase (EC 1.12.2.1) is an enzyme that catalyzes the chemical reaction
- 2 H2 + ferricytochrome c3 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 PDB: 1FRV, PDB: 1H2R, PDB: 1UBH, PDB: 1UBJ, PDB: 1UBK, PDB: 1UBL, PDB: 1UBM, PDB: 1UBO, PDB: 1UBR, PDB: 1UBT, PDB: 1UBU, PDB: 1WUH, PDB: 1WUI, PDB: 1WUJ, PDB: 1WUK, PDB: 1WUL, PDB: 1YQ9, PDB: 1YQW, and PDB: 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.
- Higuchi Y, Yasuoka N, Kakudo M, Katsube Y, Yagi T, Inokuchi H (1987). "Single crystals of hydrogenase from Desulfovibrio vulgaris Miyazaki F". J. Biol. Chem. 262 (6): 2823–5. doi:10.1016/S0021-9258(18)61580-7. PMID 3546297.
- Rilkis E; Rittenberg D (1961). "Some observations on the enzyme, hydrogenase". J. Biol. Chem. 236 (9): 2526–2529. doi:10.1016/S0021-9258(18)64033-5. 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. Bibcode:1995Natur.373..580V. doi:10.1038/373580a0. PMID 7854413. S2CID 4335445.
- 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.