Cytochrome-c3 hydrogenase

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
cytochrome-c3 hydrogenase
Identifiers
EC number1.12.2.1
CAS number9027-05-8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

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.

gollark: NCP?
gollark: Maybe something like magically driven carts. Presumably they would already have existed but were just impractical/expensive though.
gollark: Hi.
gollark: ++tel hangup
gollark: ++tel status

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. 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.
    • 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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