Compelling EPR evidence that the alternative oxidase is a diiron carboxylate protein.
Compelling EPR evidence that the alternative oxidase is a diiron carboxylate protein.
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DOI：
10.1016/j.bbabio.2008.01.004
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发表时间：
2008-04
期刊：
影响因子：
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通讯作者：
A. Moore;Jane E Carré;C. Affourtit;M. Albury;Paul G. Crichton;K. Kita;P. Heathcote
中科院分区：
文献类型：
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作者：
A. Moore;Jane E Carré;C. Affourtit;M. Albury;Paul G. Crichton;K. Kita;P. Heathcote
替代氧化酶是一种在植物、真菌和一些寄生虫中发现的呼吸链蛋白，在物理上仍然没有特征。在这份报告中，我们提出了EPR的证据，从平行模式的实验，揭示信号在约g=16，在两个纯化的替代氧化酶蛋白（g = 16.9），分离的线粒体膜（g=16.1），并在锥虫AOX大肠杆菌膜（g=16.4）中表达。这样的信号指示在酶的活性位点处的二羧酸二铁中心。据我们所知，这些数据代表了AOX在其原生环境中的第一个EPR信号。
The alternative oxidase is a respiratory chain protein found in plants, fungi and some parasites that still remains physically uncharacterised. In this report we present EPR evidence from parallel mode experiments which reveal signals at approximately g=16 in both purified alternative oxidase protein (g=16.9), isolated mitochondrial membranes (g=16.1), and in trypanosomal AOX expressed in Escherichia coli membranes (g=16.4). Such signals are indicative of a dicarboxylate diiron centre at the active site of the enzyme. To our knowledge these data represent the first EPR signals from AOX present in its native environment.