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. 1995 Feb 16;373(6515):580-7.
doi: 10.1038/373580a0.

Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas

A Volbeda  1 , M H Charon, C Piras, E C Hatchikian, M Frey, J C Fontecilla-Camps
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Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas

A Volbeda et al. Nature. .

Abstract

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 A 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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