Characterization of the Active Site of Catalytically Inactive Forms of [Nife] Hydrogenases by Density Functional Theory.
From: Instituto de Catalisis, Consejo Superior de Investigaciones Cientificas, c/ Marie Curie, 2 Campus Cantoblanco, 28049 Madrid, Spain.
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry
- Publish Date: Aug 2007
- ISSN: 0949-8257
- Volume: 12
- Issue: 6
- Pages: 751-60
- Medium: Print
- Language: English
- Citation (JAMA): Pardo Alejandro, De Lacey Antonio L, Fernández Víctor M, et al. Characterization of the Active Site of Catalytically Inactive Forms of [Nife] Hydrogenases by Density Functional Theory.. J. Biol. Inorg. Chem. Aug 2007;12:751-60
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 (mu-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 mu-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.
Mesh Headings (Keywords): Binding Sites, Enzyme Activation, Hydrogenase, Models, Molecular, Spectrum Analysis
Check for Full Text / PubMed Unique Identifier (PMID): 17440755
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