Takeshige K, Takayanagi R, Minakami S
Biochem J. 1980 Dec 15;192(3):861-6. doi: 10.1042/bj1920861.
The NADH-ubiquinone reductase preparation (Complex I) of bovine hart mitochondria catalysed in the presence of reduced coenzymes and ADP-Fe3+ the lipid peroxidation of liposomes prepared from mitochondrial lipids. The apparent Km values for the coenzymes and the optimal pH of the reactions agreed well with those of the lipid peroxidation of the submitochondrial particles treated with rotenone. On assay of the reduction of ADP-Fe3+ chelate by the reduction of cytochrome c in the presence of superoxide dismutase and antimycin A or by the oxidation of reduced coenzymes, the reactions were not affected by rotenone but were inhibited by thiol-group inhibitors. The properties of the ADP-Fe3+ reductase activity were highly consistent with those of the lipid-peroxidation reaction. These observations suggest that electrons from reduced coenzymes are transferred to ADP-Fe3+ chelate from a component between a mercurial-sensitive site and the rotenone-sensitive one of the NADH dehydrogenase and that the reduction of ADP-Fe3+ chelate by the NADH dehydrogenase is an essential step in the lipid peroxidation.
牛心脏线粒体的NADH-泛醌还原酶制剂（复合体I）在存在还原型辅酶和ADP-Fe³⁺的情况下，催化由线粒体脂质制备的脂质体的脂质过氧化反应。辅酶的表观Km值和反应的最佳pH值与用鱼藤酮处理的亚线粒体颗粒的脂质过氧化反应的相应值非常吻合。在用超氧化物歧化酶和抗霉素A存在下通过细胞色素c的还原或通过还原型辅酶的氧化来测定ADP-Fe³⁺螯合物的还原时，反应不受鱼藤酮影响，但受巯基抑制剂抑制。ADP-Fe³⁺还原酶活性的特性与脂质过氧化反应的特性高度一致。这些观察结果表明，来自还原型辅酶的电子从NADH脱氢酶的汞敏感位点和鱼藤酮敏感位点之间的一个组分转移到ADP-Fe³⁺螯合物，并且NADH脱氢酶对ADP-Fe³⁺螯合物的还原是脂质过氧化的一个必要步骤。
