Properties of a semiquinone anion located in the QH2:Cytochrome c oxidoreductase segment of the mitochondrial respiratory chain
Properties of a semiquinone anion located in the QH2:Cytochrome c oxidoreductase segment of the mitochondrial respiratory chain
复制标题
位于 QH2 的半醌阴离子的特性:线粒体呼吸链的细胞色素 c 氧化还原酶片段
DOI:
10.1016/0014-5793(80)80422-4
复制
发表时间:
1980
期刊:
影响因子:
3.5
通讯作者:
E. C. Slater
中科院分区:
文献类型:
--
作者:
S. Vries;J. Berden;E. C. Slater
The way in which electrons are transferred from ubiquinol to cytochrome c is still under discussion. The results of potentiometric titrations and measurements of the pre-steady-state kinetics monitored optically, mainly giving information on the redox properties of the cytochromes, have led to proposals [1, 2] for electron transfer through QH,: cytochrome c oxidoreductase, in which the formation of a semiquinone is a prerequisite for electron transfer. The presence of a semiquinone in preparations of the respiratory chain has, indeed, been identified by EPR studies [3-IO]. Ohnishi and Trumpower have detected two different populations of ubisemiquinone in isolated succinate: cytochrome c oxidoreductase [101, SQ, and SQ,, differing in relaxation time (see also11 r11.The results in this paper indicate the existence of a very stable semiquinone anion located in QH,: cytochrome c oxidoreductase, presumably corresponding to SQ, in [lo]. Quantitation of the EPR signal of the semiquinone anion showed that the maximal concentration is I/2 that of the cytochrome cr. In order adequately to describe the effect of pH on the semiquinone anion concentration in the Nernst equation, a Limited capacity of the binding site for the semiquinone anion must be taken into account.