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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Allosteric control of internal electron transfer in cytochrome cd(1) nitrite reductase
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Allosteric control of internal electron transfer in cytochrome cd(1) nitrite reductase

机译:细胞色素cd(1)亚硝酸盐还原酶中内部电子转移的变构控制

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Cytochrome cd(1) nitrite reductase is a bifunctional multiheme enzyme catalyzing the one-electron reduction of nitrite to nitric oxide and the four-electron reduction of dioxygen to water. Kinetics and thermodynamics of the internal electron transfer process in the Pseudomonas stutzeri enzyme have been studied and found to be dominated by pronounced interactions between the c and the d(1) hemes. The interactions are expressed both in dramatic changes in the internal electron-transfer rates between these sites and in marked cooperativity in their electron affinity. The results constitute a prime example of intraprotein control of the electron-transfer rates by allosteric interactions. [References: 15]
机译:细胞色素cd(1)亚硝酸盐还原酶是一种双功能多血红素酶,可将亚硝酸盐的单电子还原为一氧化氮,将四氧的电子还原为水。研究了斯图氏假单胞菌酶内部电子传递过程的动力学和热力学,发现其主要受c和d(1)血红素之间明显的相互作用影响。这些位点之间的内部电子传输速率发生了显着变化,并且在它们的电子亲和力中表现出明显的协同性,从而表现出相互作用。该结果构成了通过变构相互作用控制电子传递速率的蛋白内控制的主要例子。 [参考:15]

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