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Crystal structure of the nickel–iron hydrogenase from Desulfovibrio gigas

Nature volume 373, pages 580–587 (1995)Cite this article

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 Å 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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Author notes

  1. E. Claude Hatchikian: Unité de Bioénergétique et Ingéniérie des Protéines, CNRS, 13402 Marseille Cedex 20, France

  2. Michel Frey and Juan C. Fontecilla-Camps: To whom correspondence should be addressed.

Authors and Affiliations

  1. Laboratoire de Cristallographie et de Cristallogénèse des Protéines, Institut de Biologie Structurale J. P. Ebel (CEA.CNRS), 41 avenue des Martyrs, 38027, Grenoble, Cedex 1, France

    Anne Volbeda, Marie-Hélène Charon, Claudine Piras, E. Claude Hatchikian, Michel Frey & Juan C. Fontecilla-Camps

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Volbeda, A., Charon, MH., Piras, C. et al. Crystal structure of the nickel–iron hydrogenase from Desulfovibrio gigas. Nature 373, 580–587 (1995). https://doi.org/10.1038/373580a0

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