Electronic structure contributions to reactivity in xanthine oxidase family enzymes

J Biol Inorg Chem. 2015 Mar;20(2):183-94. doi: 10.1007/s00775-014-1212-8. Epub 2014 Nov 26.

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Aldehyde Oxidoreductases / chemistry*
  • Catalysis
  • Crystallography, X-Ray
  • Electron Spin Resonance Spectroscopy
  • Electrons*
  • Models, Molecular
  • Molybdenum / chemistry*
  • Multienzyme Complexes / chemistry*
  • Oxidation-Reduction
  • Protein Conformation
  • Xanthine / chemistry
  • Xanthine Oxidase / chemistry*
  • Xanthine Oxidase / classification
  • Xanthine Oxidase / metabolism

Substances

  • Multienzyme Complexes
  • Xanthine
  • Molybdenum
  • Xanthine Oxidase
  • Aldehyde Oxidoreductases
  • carbon monoxide dehydrogenase