Ferredoxin hydrogenase
| ferredoxin hydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.12.7.2 | ||||||||
| CAS number | 9080-02-8 | ||||||||
| 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 / EGO | ||||||||
| |||||||||
In enzymology, a ferredoxin hydrogenase (EC 1.12.7.2) is an enzyme that catalyzes the chemical reaction
- H2 + 2 oxidized ferredoxin
2 reduced ferredoxin + 2 H+
Thus, the two substrates of this enzyme are H2 and oxidized ferredoxin, whereas its two products are reduced ferredoxin and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on hydrogen as donor with an iron-sulfur protein as acceptor. The systematic name of this enzyme class is hydrogen:ferredoxin oxidoreductase. Other names in common use include H2 oxidizing hydrogenase, H2 producing hydrogenase [ambiguous], bidirectional hydrogenase, hydrogen-lyase [ambiguous], hydrogenase (ferredoxin), hydrogenase I, hydrogenase II, hydrogenlyase [ambiguous], and uptake hydrogenase [ambiguous]. This enzyme participates in glyoxylate and dicarboxylate metabolism and methane metabolism. It has 3 cofactors: iron, Sulfur, and Nickel.
References
- Shug AL, Wilson PW, Green DE and Mahler HR (1954). "The role of molybdenum and flavin in hydrogenase". J. Am. Chem. Soc. 76 (12): 3355–3356. doi:10.1021/ja01641a090.
- Tagawa K and Arnon DI (Lond.). "Ferredoxin as electron carriers in photosynthesis and in the bioogical production and consumption of hydrogen gas". N. Nature: 537–543. Check date values in:
|date=(help) - Valentine RC, Mortenson LE and Carnahan JE (1963). "The hydrogenase system of Clostridium pasteurianum". J. Biol. Chem. 238: 1141–1144.
- Zumft WG, Mortenson LE (1975). "The nitrogen-fixing complex of bacteria". Biochim. Biophys. Acta. 416 (1): 1–52. doi:10.1016/0304-4173(75)90012-9. PMID 164247.
- Adams MW (1990). "The structure and mechanism of iron-hydrogenases". Biochim. Biophys. Acta. 1020 (2): 115–45. PMID 2173950.
- Peters JW, Lanzilotta WN, Lemon BJ, Seefeldt LC (1998). "X-ray crystal structure of the Fe-only hydrogenase (CpI) from Clostridium pasteurianum to 1.8 angstrom resolution". Science. 282 (5395): 1853–8. doi:10.1126/science.282.5395.1853. PMID 9836629.