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Xanthine dehydrogenase electrocatalysis autocatalysis and novel activity

  • 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.

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Author details:Palraj Kalimuthu, Silke LeimkühlerORCiDGND, Paul V. Bernhardt
DOI:https://doi.org/10.1021/jp111809f
ISSN:1520-6106
Title of parent work (English):The journal of physical chemistry : B, Condensed matter, materials, surfaces, interfaces & biophysical chemistry
Publisher:American Chemical Society
Place of publishing:Washington
Publication type:Article
Language:English
Year of first publication:2011
Publication year:2011
Release date:2017/03/26
Volume:115
Issue:11
Number of pages:8
First page:2655
Last Page:2662
Funding institution:Australian Research Council [DP0880288]; Deutsche Forschungsgemeinschaft Cluster of Excellence
Organizational units:Mathematisch-Naturwissenschaftliche Fakultät / Institut für Biochemie und Biologie
Peer review:Referiert
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