恶臭假单胞菌铁氧化还原蛋白和樟脑连接对细胞色素P450cam混合功能氧化的氧化还原调节
Redox regulation of cytochrome P450cam mixed function oxidation by putidaredoxin and camphor ligation.
作者信息
Gunsalus I C, Sligar S G
出版信息
Biochimie. 1976;58(1-2):143-7. doi: 10.1016/s0300-9084(76)80364-1.
PMID:953050
Abstract
A methylene group of camphor is hydroxylated by a P450 monoxygenase system containing in addition to the cytochrome and flavoprotein dehydrogenase a two-iron, two-sulfur redox protein termed putidaredoxin. The regulatory control of electron transport equilibrium occurs via ligation of substrate and redoxin to the cytochrome. The component interactions and electron flow are represented clearly and concisely by a free energy state diagram of the coupled binding and redox transfer reactions.
摘要
樟脑的一个亚甲基被一种P450单加氧酶系统羟基化，该系统除了含有细胞色素和黄素蛋白脱氢酶外，还含有一种称为恶臭假单胞菌铁氧还蛋白的双铁双硫氧化还原蛋白。电子传递平衡的调节控制是通过底物和铁氧还蛋白与细胞色素的连接来实现的。通过耦合结合和氧化还原转移反应的自由能状态图，可以清晰简洁地表示各组分之间的相互作用和电子流。
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