Determination of the position of the Qi.- quinone binding site from the protein surface of the cytochrome bc1 complex in Rhodobacter capsulates chromatophores.
Determination of the position of the Qi.- quinone binding site from the protein surface of the cytochrome bc1 complex in Rhodobacter capsulates chromatophores.
复制标题
确定红细菌荚膜色素细胞中细胞色素 bc1 复合物蛋白质表面的 Qi.-醌结合位点的位置。
DOI：
10.1016/0005-2728(92)90127-n
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发表时间：
1992
期刊：
影响因子：
--
通讯作者：
Ohnishi,T
中科院分区：
文献类型：
--
作者：
Meinhardt,SW;Ohnishi,T
利用自旋弛豫增强由外部探针的距离测量技术已扩展到研究的内在半醌自由基通过使用的钬-EDTA络合物和连续波电子顺磁共振光谱。该技术已被用于测定半醌阴离子的距离。Q1（也称为Qn−或Qc−），来自于红细菌荚膜膜颗粒中的泛醌细胞色素氧化还原酶表面，仅由三个亚基组成。半醌阴离子的位置距离N侧蛋白质6- 10 μ m，确定存在两个独立的醌反应位点，即，'Q1'和'Q 0'，在膜的相对侧上的该复合物内。结果进行了讨论，有关报道的ENDOR，EPR，和光学研究的线粒体对应。
The technique of distance measurement utilizing spin relaxation enhancement by an external probe has been extended to the study of intrinsic semiquinone radicals through the use of holmium-EDTA complexes and continuous wave electron paramagnetic resonance spectroscopy. This technique has been used to determine the distance of the semiquinone anion. Q1(also designate as Qn−or Qc−), from the surface of the ubiquinone cytochromecoxidoreductase, consisting of only three subunits, in membrane particles fromRhodobacter capsulates. The location of the semiquinone anion is 6–10Åfrom the N side protein, establishing that there are two separate quinone reaction sites, i.e., ‘Q1’ and ‘Q0’, within this complex on opposite sides of the membrane. The results are discussed in relation to reported ENDOR, EPR, and optical studies of the mitochondrial counterpart.