Further insights into the structure of the alternative oxidase: from plants to parasites
Further insights into the structure of the alternative oxidase: from plants to parasites
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DOI：
10.1042/bst0361022
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发表时间：
2008-10-01
影响因子：
3.9
通讯作者：
Albury, Mary S.
中科院分区：
文献类型：
--
作者：
Moore, Anthony L.;Albury, Mary S.
AOX（交替氧化酶）是一种非质子动力的泛醇氧氧化还原酶，它将泛醇的氧化与水的完全还原偶联。虽然人们早就认识到它在植物界中无处不在，但直到最近才发现它也广泛存在于其他生物体中，包括一些人类寄生虫。在本文中，我们回顾了实验研究，有助于我们目前的理解其结构，特别是催化位点。此外，我们提出了一个模型的泛喹啉结合位点，它确定了一个疏水口袋，螺旋II和III之间，导致从一个拟议的膜结合域的催化域。
The AOX (alternative oxidase) is a non-proton motive ubiquinol-oxygen oxidoreductase that couples the oxidation of ubiquinol with the complete reduction of water. Although it has long been recognized that it is ubiquitous among the plant kingdom, it has only recently become apparent that it is also widely found in other organisms including some human parasites. in this paper, we review experimental studies that have contributed to our current understanding of its structure, with particular reference to the catalytic site. Furthermore, we propose a model for the ubiquinol-binding site which identifies a hydrophobic pocket, between helices II and III, leading from a proposed membrane-binding domain to the catalytic domain.