High-affinity iron binding by xanthine oxidase

Glenn F. Vile, Christine C. Winterbourn
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引用次数: 5

Abstract

Equilibrium dialysis studies on competitive binding of 59FeCl3 to xanthine oxidase and citrate or ATP have been carried out. Iron binding to the enzyme was observed in the presence of 0.1 mM of either chelator, suggesting that xanthine oxidase is likely to have iron bound in many in vitro experimental systems and raising the possibility that it may be able to compete for intracellular chelatable iron. One high-affinity-binding site per monomer was found, with an affinity constant of 5 × 1012 M−1. The significance of this iron as a Fenton reaction catalyst is discussed.

黄嘌呤氧化酶高亲和铁结合
平衡透析研究了59FeCl3与黄嘌呤氧化酶、柠檬酸盐或ATP的竞争结合。在任何一种螯合剂存在0.1 mM的情况下,观察到铁与酶的结合,这表明在许多体外实验系统中,黄嘌呤氧化酶可能与铁结合,并提高了它可能能够竞争细胞内螯合铁的可能性。每个单体发现一个高亲和结合位点,亲和常数为5 × 1012 M−1。讨论了该铁作为芬顿反应催化剂的意义。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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