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
Matsuno-Yagi, A
中科院分区:
生物学3区
文献类型:
--
作者:
Yagi, T;Matsuno-Yagi, A

文献摘要

被引文献

相似文献

哺乳动物线粒体的呼吸链由四种酶复合物组成,如图1所示。这些复合物都位于哺乳动物的线粒体内膜中,被称为质子转运NADH-醌氧化还原酶(复合物I)、琥珀酸-醌氧化还原酶(复合物II)、bc 1复合物(复合物III)和细胞色素c氧化酶(复合物IV)。复合物I由至少46个不同的亚基(1)组成,总分子量约为1 MDa。这种酶复合物跨越线粒体内膜,带有一个非共价结合的FMN和八个铁硫簇(2)。它将质子从膜的基质侧转移到细胞质侧,产生穿过线粒体内膜的质子梯度。由于复合物I能够与底物的氧化一起泵送质子,因此它构成了氧化磷酸化系统的能量偶联位点1。除了存在于哺乳动物线粒体中,复合物I也存在于植物和真菌线粒体中
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