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 Å resolution. The active site, which appears to contain, besides nickel, a second metal ion, is buried in the 60K subunit. The...

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Veröffentlicht in:	Nature (London) 1995-02, Vol.373 (6515), p.580-587
Hauptverfasser:	Volbeda, Anne, Charon, Marie-Hélène, Piras, Claudine, Hatchikian, E. Claude, Frey, Michel, Fontecilla-Camps, Juan C
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Bacteriology Binding Sites Biological and medical sciences Computer Graphics Crystallography, X-Ray Crystals Desulfovibrio - enzymology Desulfovibrio gigas Electron Transport Enzymes Fundamental and applied biological sciences. Psychology Humanities and Social Sciences Hydrogenase - chemistry Hydrogenase - metabolism Ions Iron Iron - chemistry Iron-Sulfur Proteins - chemistry Metabolism Metabolism. Enzymes Microbiology Molecular Sequence Data multidisciplinary Nickel Nickel - chemistry Protein Conformation Protein Processing, Post-Translational Protons Science Science (multidisciplinary)
Online-Zugang:	Volltext
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