Palraj Kalimuthu, Silke Leimkühler, Paul V Bernhardt
School of Chemistry and Molecular Biosciences, University of Queensland, Brisbane 4072, Australia.
The journal of physical chemistry. B 2012 Sep 27We report the mediated electrocatalytic voltammetry of the molybdoenzyme xanthine dehydrogenase (XDH) from Rhodobacter capsulatus at a thiol-modified Au electrode. The 2-electron acceptor N-methylphenazinium methanesulfonate (phenazine methosulfate, PMS) is an effective artificial electron transfer partner for XDH instead of its native electron acceptor NAD(+). XDH catalyzes the oxidative hydroxylation of hypoxanthine to xanthine and xanthine to uric acid. Cyclic voltammetry was used to generate the active (oxidized) form of the mediator. Simulation of the catalytic voltammetry across a broad range of substrate and PMS concentrations at different sweep rates was achieved with the program DigiSim to yield a set of consistent rate and equilibrium constants that describe the catalytic system. This provides the first example of the mediated electrochemistry of a xanthine dehydrogenase (or oxidase) that is uncomplicated by interference from product oxidation. A remarkable two-step, sequential oxidation of hypoxanthine to uric acid via xanthine by XDH is observed.
Palraj Kalimuthu, Silke Leimkühler, Paul V Bernhardt. Catalytic electrochemistry of xanthine dehydrogenase. The journal of physical chemistry. B. 2012 Sep 27;116(38):11600-7
PMID: 22934570
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