KINETICS, CONTROL, AND MECHANISM OF UBIQUINONE REDUCTION BY THE MAMMALIAN RESPIRATORY CHAIN-LINKED NADH-UBIQUINONE REDUCTASE

被引:76
作者
VINOGRADOV, AD
机构
[1] Department of Biochemistry, School of Biology, Moscow State University, Moscow
关键词
NADH-UBIQUINONE OXIDOREDUCTASE; UBISEMIQUINONE; FLAVIN; ELECTRON TRANSFER; ENZYME HYSTERESIS; IRON-SULFUR CLUSTERS; MITOCHONDRIA;
D O I
10.1007/BF00762462
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
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.
引用
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页码:367 / 375
页数:9
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