Vinogradov A D, Grivennikova V G
Department of Biochemistry, School of Biology, Moscow State University, Russian Federation.
IUBMB Life. 2001 Sep-Nov;52(3-5):129-34. doi: 10.1080/15216540152845920.
Although the mitochondrial Complex I has been extensively studied for over 4 decades, its catalytic properties in mitochondria are poorly understood. This review summarizes the data on standard and nonstandard kinetic parameters of the enzyme. The slow interconversion between active and deactivated forms of the mammalian Complex I (A/D transition) is described. We discuss the potential relevance of this transition for the regulation of NADH oxidation by the respiratory chain under physiological and pathophysiological conditions.
尽管线粒体复合物I已经被广泛研究了40多年，但人们对其在线粒体中的催化特性却知之甚少。这篇综述总结了关于该酶的标准和非标准动力学参数的数据。描述了哺乳动物复合物I活性和失活形式之间缓慢的相互转化（A/D转变）。我们讨论了这种转变在生理和病理生理条件下对呼吸链调节NADH氧化的潜在相关性。
