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.
Author details: | Palraj Kalimuthu, Silke LeimkühlerORCiDGND, Paul V. Bernhardt |
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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 |