Kerscher Stefan, Dröse Stefan, Zickermann Volker, Brandt Ulrich
Molecular Bioenergetics Group, Centre of Excellence Macromolecular Complexes, Johann Wolfgang Goethe-Universität, 60590, Frankfurt am Main, Germany.
Results Probl Cell Differ. 2008;45:185-222. doi: 10.1007/400_2007_028.
Most reducing equivalents extracted from foodstuffs during oxidative metabolism are fed into the respiratory chains of aerobic bacteria and mitochondria by NADH:quinone oxidoreductases. Three families of enzymes can perform this task and differ remarkably in their complexity and role in energy conversion. Alternative or NDH-2-type NADH dehydrogenases are simple one subunit flavoenzymes that completely dissipate the redox energy of the NADH/quinone couple. Sodium-pumping NADH dehydrogenases (Nqr) that are only found in procaryotes contain several flavins and are integral membrane protein complexes composed of six different subunits. Proton-pumping NADH dehydrogenases (NDH-1 or complex I) are highly complicated membrane protein complexes, composed of up to 45 different subunits, that are found in bacteria and mitochondria. This review gives an overview of the origin, structural and functional properties and physiological significance of these three types of NADH dehydrogenase.
在氧化代谢过程中,从食物中提取的大多数还原当量通过NADH:醌氧化还原酶被输入到需氧细菌和线粒体的呼吸链中。有三类酶可以执行这项任务,它们在复杂性和能量转换作用方面有显著差异。交替型或NDH-2型NADH脱氢酶是简单的单亚基黄素酶,可完全消耗NADH/醌对的氧化还原能量。仅在原核生物中发现的钠泵NADH脱氢酶(Nqr)含有几种黄素,是由六个不同亚基组成的完整膜蛋白复合物。质子泵NADH脱氢酶(NDH-1或复合体I)是高度复杂的膜蛋白复合物,由多达45个不同亚基组成,存在于细菌和线粒体中。本综述概述了这三种类型NADH脱氢酶的起源、结构和功能特性以及生理意义。