The Enzyme Database

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EC 1.12.7.2     
Accepted name: ferredoxin hydrogenase
Reaction: H2 + 2 oxidized ferredoxin = 2 reduced ferredoxin + 2 H+
Other name(s): H2 oxidizing hydrogenase; H2 producing hydrogenase [ambiguous]; bidirectional hydrogenase; hydrogen-lyase [ambiguous]; hydrogenase (ferredoxin); hydrogenase I; hydrogenase II; hydrogenlyase [ambiguous]; uptake hydrogenase [ambiguous]
Systematic name: hydrogen:ferredoxin oxidoreductase
Comments: Contains iron-sulfur clusters. The enzymes from some sources contains nickel. Can use molecular hydrogen for the reduction of a variety of substances.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, UM-BBD, CAS registry number: 9027-05-8
References:
1.  Shug, A.L., Wilson, P.W., Green, D.E. and Mahler, H.R. The role of molybdenum and flavin in hydrogenase. J. Am. Chem. Soc. 76 (1954) 3355–3356.
2.  Tagawa, K. and Arnon, D.I. Ferredoxin as electron carriers in photosynthesis and in the bioogical production and consumption of hydrogen gas. Nature (Lond.) 195 (1962) 537–543.
3.  Valentine, R.C., Mortenson, L.E. and Carnahan, J.E. The hydrogenase system of Clostridium pasteurianum. J. Biol. Chem. 238 (1963) 1141–1144.
4.  Zumft, W.G. and Mortenson, L.E. The nitrogen-fixing complex of bacteria. Biochim. Biophys. Acta 416 (1975) 1–52. [PMID: 164247]
5.  Adams, M.W.W. The structure and mechanism of iron-hydrogenases. Biochim. Biophys. Acta 1020 (1990) 115–145. [PMID: 2173950]
6.  Peters, J.W., Lanzilotta, W.N., Lemon, B.J. and Seefeldt, L.C. X-ray crystal structure of the Fe-only hydrogenase (Cpl) from Clostridium pasteurianum to 1.8 Angstrom resolution. Science 282 (1998) 1853–1858. [PMID: 9836629]
[EC 1.12.7.2 created 1961 as EC 1.98.1.1, transferred 1965 to EC 1.12.1.1, transferred 1972 to EC 1.12.7.1, transferred 1978 to EC 1.18.3.1, transferred 1984 to EC 1.18.99.1, transferred 2002 to EC 1.12.7.2]
 
 


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