Characterization of ubisemiquinone radical in the cytochrome b-c1 segment of the mitochondrial respiratory chain.
Characterization of ubisemiquinone radical in the cytochrome b-c1 segment of the mitochondrial respiratory chain.
复制标题
线粒体呼吸链细胞色素 b-c1 片段中泛半醌自由基的表征。
DOI:
10.1016/0003-9861(81)90517-8
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发表时间:
1981
影响因子:
3.9
通讯作者:
King,TE
中科院分区:
文献类型:
--
作者:
Nagaoka,S;Yu,L;King,TE
The ubiquinone protein, QP-C, in reduced ubiquinone-cytochrome c reductase (the b− c 1-III complex) shows a stable ubisemiquinone radical when the enzyme is reduced by succinate in the presence of catalytic amounts of succinate dehydrogenase and QP-S. At room temperature using EPR technique the redox titration of the b− c 1-III complex in the presence of redox dyes or succinate/fumarate couple reveals that the ubisemiquinone radical has a midpoint potential of approximately+ 67 mV at pH 8.0. Further analysis yields E 1 of+ 83 mV and E 2 of+ 51 mV corresponding to (QH 2 QH·) and (QH· Q) or other electronated forms, respectively. The equilibrium radical concentration has been found to be affected both by pH and succinate/fumarate couple. At pH 9.0 the radical shows the maximal amplitude and stability. Below pH 7.0, little radical was detected. The electron spin relaxation behavior of ubisemiquinone radical, as examined by microwave power saturation, indicates that the ubisemiquinone radical of QP-C is somewhat isolated from other paramagnetic centers. The effects of phospholipids, QP-S, and other agents on ubisemiquinone radical formation as well as the enzymatic activity of QP-C have been studied in detail.