Cytochrome-c3 hydrogenase

In enzymology, a cytochrome-c3 hydrogenase (EC 1.12.2.1) is an enzyme that catalyzes the chemical reaction

cytochrome-c3 hydrogenase
Identifiers
EC no.	1.12.2.1
CAS no.	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
Search PMC articles PubMed articles NCBI proteins

2 H₂ + ferricytochrome c₃ $\rightleftharpoons$ 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.
• 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.