蛋白质亚单位
线粒体基质
线粒体
辅酶Q-细胞色素c还原酶
生物化学
细胞色素C1
生物
细胞色素c
酶
化学
细胞生物学
胞浆
基因
作者
So Iwata,Joong W. Lee,Kengo Okada,John Kyongwon Lee,Momi Iwata,Bjarne Rasmussen,Thomas Link,S. Ramaswamy,Bing K. Jap
出处
期刊:Science
[American Association for the Advancement of Science]
日期:1998-07-03
卷期号:281 (5373): 64-71
被引量:1185
标识
DOI:10.1126/science.281.5373.64
摘要
Mitochondrial cytochrome bc 1 complex performs two functions: It is a respiratory multienzyme complex and it recognizes a mitochondrial targeting presequence. Refined crystal structures of the 11-subunit bc 1 complex from bovine heart reveal full views of this bifunctional enzyme. The “Rieske” iron-sulfur protein subunit shows significant conformational changes in different crystal forms, suggesting a new electron transport mechanism of the enzyme. The mitochondrial targeting presequence of the “Rieske” protein (subunit 9) is lodged between the two “core” subunits at the matrix side of the complex. These “core” subunits are related to the matrix processing peptidase, and the structure unveils how mitochondrial targeting presequences are recognized.
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