The proton-translocating NADH-quinone oxidoreductase in the respiratory chain: The secret unlocked
The proton-translocating NADH-quinone oxidoreductase in the respiratory chain: The secret unlocked
复制标题
DOI:
10.1021/bi027158b
复制
发表时间:
2003-03-04
期刊:
影响因子:
2.9
通讯作者:
Matsuno-Yagi, A
中科院分区:
文献类型:
--
作者:
Yagi, T;Matsuno-Yagi, A
The respiratory chain of mammalian mitochondria is composed of four enzyme complexes as depicted in Figure 1. These complexes, which are all located in the mammalian inner-mitochondrial membrane, are referred to as the protontranslocating NADH-quinone oxidoreductase (complex I), 1 the succinate-quinone oxidoreductase (complex II), the bc1 complex (complex III), and cyt c oxidase (complex IV). Complex I is composed of at least 46 different subunits (1) with a total molecular mass of approximately 1 MDa. This enzyme complex, which spans the inner-mitochondrial membrane, bears one noncovalently bound FMN and eight iron-sulfur clusters (2). It translocates protons from the matrix side of the membrane to the cytoplasmic side, generating a proton gradient across the inner-mitochondrial membrane. Because of its ability to pump protons in concert with oxidation of a substrate, complex I constitutes the energy coupling site 1 of the oxidative phosphorylation system. In addition to being present in mammalian mitochondria, complex I is also present in plant and fungal mitochondria