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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Coenzyme Q reductase from liver plasma membrane: purification and role in trans-plasma-membrane electron transport.
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Coenzyme Q reductase from liver plasma membrane: purification and role in trans-plasma-membrane electron transport.

机译：肝脏质膜上的辅酶Q还原酶：纯化及其在跨质膜电子传输中的作用。

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摘要

A specific requirement for coenzyme Q in the maintenance of trans-plasma-membrane redox activity is demonstrated. Extraction of coenzyme Q from membranes resulted in inhibition of NADH-ascorbate free radical reductase (trans electron transport), and addition of coenzyme Q10 restored the activity. NADH-cytochrome c oxidoreductase (cis electron transport) did not respond to the coenzyme Q status. Quinone analogs inhibited trans-plasma-membrane redox activity, and the inhibition was reversed by coenzyme Q. A 34-kDa coenzyme Q reductase (p34) has been purified from pig-liver plasma membranes. The isolated enzyme was sensitive to quinone-site inhibitors. p34 catalyzed the NADH-dependent reduction of coenzyme Q10 after reconstitution in phospholipid liposomes. When plasma membranes were supplemented with extra p34, NADH-ascorbate free radical reductase was activated but NADH-cytochrome c oxidoreductase was not. These results support the involvement of p34 as a source of electrons for the trans-plasma-membrane redox system oxidizing NADH and support coenzyme Q as an intermediate electron carrier between NADH and the external acceptor ascorbate free radical.
机译：证明了在维持跨质膜氧化还原活性中对辅酶Q的特殊要求。从膜中提取辅酶Q会抑制NADH-抗坏血酸自由基还原酶（反式电子传输），添加辅酶Q10可恢复活性。 NADH-细胞色素c氧化还原酶（顺式电子传输）不响应辅酶Q的状态。醌类似物抑制跨质膜氧化还原活性，并且该抑制作用被辅酶Q逆转。一种34 kDa的辅酶Q还原酶（p34）已从猪肝血浆膜中纯化出来。分离的酶对醌位抑制剂敏感。在磷脂脂质体中重构后，p34催化了辅酶Q10的NADH依赖性还原。当质膜中添加额外的p34时，NADH-抗坏血酸自由基还原酶被激活，而NADH-细胞色素c氧化还原酶则未被激活。这些结果支持p34作为氧化NADH的跨质膜氧化还原系统的电子源的参与，并支持辅酶Q作为NADH与外部受体抗坏血酸自由基之间的中间电子载体。

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