Multicopper oxidases: intramolecular electron transfer and O2 reduction
Multicopper oxidases: intramolecular electron transfer and O2 reduction
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DOI：
10.1007/s00775-013-1080-7
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发表时间：
2014-01
期刊：
影响因子：
--
通讯作者：
S. Wherland;O. Farver;I. Pecht
中科院分区：
文献类型：
--
作者：
S. Wherland;O. Farver;I. Pecht
多铜氧化物酶是一个有趣的、分布广泛的酶家族，它催化各种单电子和多电子还原剂将O2还原为水。引起后一种化学转变的铜结合位的结构和性质已经研究了40多年，详细的图景正在显现。本文着重讨论了第一类(蓝色)铜中心和三核中心之间的内部电子转移动力学，以及氧还原过程中形成的中间产物的性质。
The multicopper oxidases are an intriguing, widespread family of enzymes that catalyze the reduction of O2to water by a variety of single-electron and multiple-electron reducing agents. The structure and properties of the copper binding sites responsible for the latter chemical transformations have been studied for over 40 years and a detailed picture is emerging. This review focuses particularly on the kinetics of internal electron transfer between the type 1 (blue) copper site and the trinuclear center, as well as on the nature of the intermediates formed in the oxygen reduction process.