Xanthine dehydrogenase electrocatalysis: autocatalysis and novel activity

J Phys Chem B. 2011 Mar 24;115(11):2655-62. doi: 10.1021/jp111809f. Epub 2011 Mar 1.

Abstract

The enzyme xanthine dehydrogenase (XDH) from the purple photosynthetic bacterium Rhodobacter capsulatus catalyzes the oxidation of hypoxanthine to xanthine and xanthine to uric acid as part of purine metabolism. The native electron acceptor is NAD(+) but herein we show that uric acid in its 2-electron oxidized form is able to act as an artificial electron acceptor from XDH in an electrochemically driven catalytic system. Hypoxanthine oxidation is also observed with the novel production of uric acid in a series of two consecutive 2-electron oxidation reactions via xanthine. XDH exhibits native activity in terms of its pH optimum and inhibition by allopurinol.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Allopurinol / chemistry
  • Biocatalysis*
  • Electrochemistry
  • Electrodes
  • Flavin-Adenine Dinucleotide / chemistry
  • Hydrogen-Ion Concentration
  • Hypoxanthine / chemistry
  • Imines / chemistry
  • NAD / chemistry
  • Oxidation-Reduction
  • Rhodobacter capsulatus / chemistry
  • Uric Acid / analogs & derivatives
  • Uric Acid / chemistry
  • Xanthine / chemistry
  • Xanthine Dehydrogenase / antagonists & inhibitors
  • Xanthine Dehydrogenase / chemistry*

Substances

  • Imines
  • NAD
  • Flavin-Adenine Dinucleotide
  • Xanthine
  • Uric Acid
  • Hypoxanthine
  • Allopurinol
  • Xanthine Dehydrogenase