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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas.

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.[1]

References

  1. Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas. Volbeda, A., Charon, M.H., Piras, C., Hatchikian, E.C., Frey, M., Fontecilla-Camps, J.C. Nature (1995) [Pubmed]
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