Characterization of the active site of catalytically inactive forms of [NiFe] hydrogenases by density functional theory |
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Authors: | Alejandro Pardo Antonio L. De Lacey Víctor M. Fernández Yubo Fan Michael B. Hall |
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Affiliation: | (1) Instituto de Catalisis, CSIC, c/ Marie Curie, 2, Campus Cantoblanco, 28049 Madrid, Spain;(2) Department of Chemistry, Texas A&M University, 3255 TAMU, College Station, TX 77843-3255, USA |
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Abstract: | The inactive forms, unready (Ni-A, Ni-SU) and ready (Ni-B), of NiFe hydrogenases are modeled by examining the possibility of hydroxo, oxo, hydroperoxo, peroxo, and sulfenate groups in active-site models and comparing predicted IR frequencies and g tensors with those of the enzyme. The best models for Ni-A and Ni-SU have hydroxo (μ-OH) bridges between Fe and Ni and a terminal sulfenate [Ni–S(=O)Cys] group, although a hydroperoxo model for Ni-A is also quite viable, whereas the best model for Ni-B has only a μ-OH bridge. In addition, a mechanism for the activation of unready hydrogenase is proposed on the basis of the relative stabilities of sulfenate models versus peroxide models. |
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Keywords: | [NiFe] hydrogenases Density functional theory Oxidized forms Quantum mechanics |
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