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Xanthine dehydrogenase electrocatalysis: autocatalysis and novel activity.
J Phys Chem B. 2011 Mar 24; 115(11):2655-62.JP

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.

Authors+Show Affiliations

Centre for Metals in Biology, School of Chemistry and Molecular Biosciences, University of Queensland , Brisbane, 4072, Australia and.No affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

21361328

Citation

Kalimuthu, Palraj, et al. "Xanthine Dehydrogenase Electrocatalysis: Autocatalysis and Novel Activity." The Journal of Physical Chemistry. B, vol. 115, no. 11, 2011, pp. 2655-62.
Kalimuthu P, Leimkühler S, Bernhardt PV. Xanthine dehydrogenase electrocatalysis: autocatalysis and novel activity. J Phys Chem B. 2011;115(11):2655-62.
Kalimuthu, P., Leimkühler, S., & Bernhardt, P. V. (2011). Xanthine dehydrogenase electrocatalysis: autocatalysis and novel activity. The Journal of Physical Chemistry. B, 115(11), 2655-62. https://doi.org/10.1021/jp111809f
Kalimuthu P, Leimkühler S, Bernhardt PV. Xanthine Dehydrogenase Electrocatalysis: Autocatalysis and Novel Activity. J Phys Chem B. 2011 Mar 24;115(11):2655-62. PubMed PMID: 21361328.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Xanthine dehydrogenase electrocatalysis: autocatalysis and novel activity. AU - Kalimuthu,Palraj, AU - Leimkühler,Silke, AU - Bernhardt,Paul V, Y1 - 2011/03/01/ PY - 2011/3/3/entrez PY - 2011/3/3/pubmed PY - 2011/8/30/medline SP - 2655 EP - 62 JF - The journal of physical chemistry. B JO - J Phys Chem B VL - 115 IS - 11 N2 - 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. SN - 1520-5207 UR - https://www.unboundmedicine.com/medline/citation/21361328/Xanthine_dehydrogenase_electrocatalysis:_autocatalysis_and_novel_activity_ L2 - https://doi.org/10.1021/jp111809f DB - PRIME DP - Unbound Medicine ER -