Centre for Metals in Biology, School of Chemistry and Molecular Biosciences, University of Queensland , Brisbane, 4072, Australia and.
J Phys Chem B. 2011 Mar 24;115(11):2655-62. doi: 10.1021/jp111809f. Epub 2011 Mar 1.
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.
来自紫色光合细菌荚膜红细菌的黄嘌呤脱氢酶（XDH）作为嘌呤代谢的一部分，催化次黄嘌呤氧化为黄嘌呤，黄嘌呤氧化为尿酸。天然的电子受体是 NAD(+)，但本文显示，尿酸的 2 电子氧化形式能够在电化学驱动的催化体系中充当 XDH 的人工电子受体。通过黄嘌呤的两次连续 2 电子氧化反应，也观察到了次黄嘌呤的氧化和尿酸的新型生成。XDH 表现出其最适 pH 值和别嘌呤醇抑制的天然活性。
