Vinogradov A D
Department of Biochemistry, School of Biology, Moscow State University, Russia.
J Bioenerg Biomembr. 1993 Aug;25(4):367-75. doi: 10.1007/BF00762462.
In mammalian cells the membrane-bound NADH-quinone oxidoreductase serves as the entry point for oxidation of NADH in the respiratory chain and as the proton-translocating unit which conserves the free energy of the enzyme intramolecular redox reactions as the free energy of the electrochemical proton gradient across the coupling membrane. This review summarizes the kinetic properties of the mammalian enzyme. Emphasis is placed on the hysteretic properties of the enzyme as related to the possible control of intramitochondrial NADH oxidation and to the mechanism of the enzyme interaction with ubiquinone. Recent evidence for participation of flavin and the protein-bound ubisemiquinone pair in the enzyme-catalyzed proton translocation mechanism are discussed.
在哺乳动物细胞中，膜结合的NADH-醌氧化还原酶是呼吸链中NADH氧化的入口点，也是质子转运单元，它将酶分子内氧化还原反应的自由能转化为跨偶联膜的电化学质子梯度的自由能。本综述总结了哺乳动物酶的动力学特性。重点讨论了该酶的滞后特性，这与线粒体内NADH氧化的可能调控以及酶与泛醌的相互作用机制有关。还讨论了黄素和与蛋白质结合的半醌对参与酶催化质子转运机制的最新证据。
