Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas.
Volbeda, Anne; Charon, Marie-Helene; Piras, Claudine; Hatchikian, E. Claude; Frey, Michel; Fontecilla-Camps, Juan C.
[Article] Nature. 373(6515):580-586, February 16, 1995.

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The X-ray structure of the heterodimeric Ni-Fe hydrogenase from Desulfovibrio gigas, the enzyme responsible for the metabolism of molecular hydrogen, has been solved at 2.85 Angstrom resolution. The active site, which appears to contain, besides nickel, a second metal ion, is buried in the 60K subunit. The 28K subunit, which coordinates one [3Fe-4S] and two [4Fe-4S] clusters, contains an amino-terminal domain with similarities to the redox protein flavodoxin. The structure suggests plausible electron and proton transfer pathways.

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