Electronic structure contributions to reactivity in xanthine oxidase family enzymes.

Martin L Kirk, Benjamin W Stein

Journal: Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry 2016;20(2):183-94

PMID: 25425163

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Abstract

We review the xanthine oxidase (XO) family of pyranopterin molybdenum enzymes with a specific emphasis on electronic structure contributions to reactivity. In addition to xanthine and aldehyde oxidoreductases, which catalyze the two-electron oxidation of aromatic heterocycles and aldehyde substrates, this mini-review highlights recent work on the closely related carbon monoxide dehydrogenase (CODH) that catalyzes the oxidation of CO using a unique Mo-Cu heterobimetallic active site. A primary focus of this mini-review relates to how spectroscopy and computational methods have been used to develop an understanding of critical relationships between geometric structure, electronic structure, and catalytic function.

Address: Department of Chemistry and Chemical Biology, University of New Mexico, MSC03 2060, 300 Terrace St. NE, Albuquerque, NM, 87131, USA.

DOI: 10.1007/s00775-014-1212-8

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MeSH Terms: Aldehyde Oxidoreductases, Catalysis, Crystallography, X-Ray, Electron Spin Resonance Spectroscopy, Electrons, Models, Molecular, Molybdenum, Multienzyme Complexes, Oxidation-Reduction, Protein Conformation, Xanthine, Xanthine Oxidase