硫代硝基苯甲酸修饰的酵母细胞色素c与牛心细胞色素c氧化酶单体和二聚体形式的反应。
Reaction of thionitrobenzoate-modified yeast cytochrome c with monomeric and dimeric forms of beef heart cytochrome c oxidase.
作者信息
Darley-Usmar V M, Georgevich G, Capaldi R A
出版信息
FEBS Lett. 1984 Jan 23;166(1):131-5. doi: 10.1016/0014-5793(84)80058-7.
PMID:6319188
Abstract
Thionitrobenzoate-modified yeast cytochrome c was shown to react with both monomeric and dimeric forms of beef heart cytochrome c oxidase through subunit III. This cytochrome c derivative was found to inhibit electron transfer in the dimer but not in the monomer. These results are interpreted to show that the high affinity binding site for cytochrome c is a cleft at the interface between monomers in the cytochrome c oxidase dimer.
摘要
硫代硝基苯甲酸修饰的酵母细胞色素c被证明可通过亚基III与牛心细胞色素c氧化酶的单体和二聚体形式发生反应。发现这种细胞色素c衍生物可抑制二聚体中的电子传递，但不能抑制单体中的电子传递。这些结果被解释为表明细胞色素c的高亲和力结合位点是细胞色素c氧化酶二聚体中单体之间界面处的一个裂隙。
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