Evidence for selenocysteine coordination to the active site nickel in the [NiFeSe]hydrogenases from Desulfovibrio baculatus
| Autor: | Daniel V. DerVartanian, José J. G. Moura, Marly K. Eidsness, Isabel Moura, Jean LeGall, Benet C. Prickril, Harry D. Peck, Robert A. Scott |
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| Přispěvatelé: | Instituto de Tecnologia Química e Biológica António Xavier (ITQB) |
| Předmět: |
Hydrogenase
Protein Conformation Iron Inorganic chemistry chemistry.chemical_element Catalysis chemistry.chemical_compound Selenium Nickel Cysteine General Multidisciplinary Binding Sites biology Selenocysteine Ligand Spectrum Analysis Active site Metalloendopeptidases biology.organism_classification Desulfovibrio Crystallography chemistry biology.protein Oxidation-Reduction Research Article |
| Zdroj: | Ciência Vitae Scopus-Elsevier |
| Popis: | Ni and Se x-ray absorption spectroscopic studies of the [NiFeSe]hydrogenases from Desulfovibrio baculatus are described. The Ni site geometry is pseudo-octahedral with a coordinating ligand composition of 3-4 (N,O) at 2.06 A, 1-2 (S,Cl) at 2.17 A, and 1 Se at 2.44 A. The Se coordination environment consists of 1 C at 2.0 A and a heavy scatterer M (M = Ni or Fe) at approximately 2.4 A. These results are interpreted in terms of a selenocysteine residue coordinated to the Ni site. The possible role of the Ni-Se site in the catalytic activation of H2 is discussed. publishersversion published |
| Databáze: | OpenAIRE |
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