Structural and functional features of the interaction of cytochrome c with complex III and cytochrome c oxidase-猫眼课题宝

细胞色素c与复合物III和细胞色素c氧化酶相互作用的结构和功能特征

DOI：

10.1016/0014-5793(82)80382-7

发表时间：

1982

期刊：

FEBS Letters

影响因子：

3.5

通讯作者：

中科院分区：

生物学3区

文献类型：

作者：

R. Capaldi;Victor M. Darley;Stephen D. Fuller;F. Millett

Cytochrome c was the first respiratory protein of mitochondria to be isolated in pure form. The water solubility and stability of this hemoprotein has made for ease of study and cytochrome c is one of the best characterized proteins in the cell. The primary structure of cytochrome c from a multitude of different sources has been determined. The protein has been crystallized and three-dimensional structural information obtained by X-ray studies [l-3]. For tuna cytochrome c, the structure of the oxidized and reduced states of the protein have been determined and refined to 1 S-1.8 A; a resolution at which bond angles and bond lengths between individual atoms can be measured [4]. In addition to these structural studies, there has been considerable work on the kinetics of electron transfer between cytochrome c and artificial electron donors and acceptors such as ferrocyanide [5-l 01. Based on these experiments, precise mechanisms of electron transfer between small molecule electron donors and cytochrome c have been proposed [9-l 11. plex III and cytochrome c oxidase and considers the implications of these results for our understanding of the terminal steps in mitochondrial electron transport.