Reconstitution of succinate-coenzyme Q reductase (complex II) and succinate oxidase activities by a highly purified, reactivated succinate dehydrogenase.
Reconstitution of succinate-coenzyme Q reductase (complex II) and succinate oxidase activities by a highly purified, reactivated succinate dehydrogenase.
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通过高度纯化、重新激活的琥珀酸脱氢酶重建琥珀酸辅酶 Q 还原酶（复合物 II）和琥珀酸氧化酶活性。
DOI：
10.1016/s0021-9258(18)63662-2
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发表时间：
1969
期刊：
影响因子：
--
通讯作者：
Y. Hatefi
中科院分区：
文献类型：
--
作者：
M. Baginsky;Y. Hatefi
琥珀酸脱氢酶已从琥珀酸辅酶Q还原酶制剂中以高度纯化的形式分离出来。每150，000克蛋白质中含有1摩尔共价结合的黄素、8克铁原子和8摩尔酸不稳定硫化物。在吩嗪硫酸甲酯作为电子受体的情况下，以26至32 µ mol/minxmg蛋白质的速率催化琥珀酸氧化（Vpmsmax ≥ 37）。如此制备的琥珀酸脱氢酶不与电子传递系统偶联，但可以在用Na 2S、亚铁离子和巯基乙醇处理后使其与电子传递系统偶联。因此，琥珀酸-辅酶Q还原酶和琥珀酸氧化酶系统都通过将再活化的琥珀酸脱氢酶与呼吸链的适当片段结合而重建。这些结果允许更好地理解线粒体呼吸链的组成和电子传递途径从琥珀酸辅酶Q。
Succinate dehydrogenase has been isolated in a highly purified form from succinate-coenzyme Q reductase preparations. The enzyme contains 1 mole of covalently bound flavin, 8 g atoms of iron, and 8 moles of acid-labile sulfide per 150,000 g of protein. It catalyzes succinate oxidation in the presence of phenazine methosulfate as electron acceptor at a rate of 26 to 32 µmoles per minxmg of protein (Vpmsmax≃ 37). The succinate dehydrogenase thus prepared does not couple to the electron transport system, but it can be made to do so after treatment with Na2S, ferrous ions, and mercaptoethanol. Thus, both the succinate-coenzyme Q reductase and the succinoxidase systems have been reconstituted by combining the reactivated succinate dehydrogenase with appropriate segments of the respiratory chain. These results permit a better understanding of the composition and the electron transfer pathway of the mitochondrial respiratory chain from succinate to coenzyme Q.