细胞色素cd1亚硝酸还原酶内部电子转移的变构调控
Allosteric control of internal electron transfer in cytochrome cd1 nitrite reductase.
作者信息
Farver Ole, Kroneck Peter M H, Zumft Walter G, Pecht Israel
机构信息
Department of Analytical Chemistry, Danish University of Pharmaceutical Sciences, DK-2100 Copenhagen, Denmark.
出版信息
Proc Natl Acad Sci U S A. 2003 Jun 24;100(13):7622-5. doi: 10.1073/pnas.0932693100. Epub 2003 Jun 11.
Abstract
Cytochrome cd1 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 d1 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.
摘要
细胞色素cd1亚硝酸还原酶是一种双功能多血红素酶，催化亚硝酸单电子还原为一氧化氮以及氧气四电子还原为水。人们已经研究了施氏假单胞菌中该酶内部电子转移过程的动力学和热力学，发现其主要受c型和d1型血红素之间显著相互作用的支配。这些相互作用既表现为这些位点之间内部电子转移速率的剧烈变化，也表现为它们电子亲和力的显著协同性。这些结果构成了通过变构相互作用对蛋白质内电子转移速率进行控制的一个典型例子。
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