膜结合硝酸还原酶氧化还原中心的协调作用与功能。
The coordination and function of the redox centres of the membrane-bound nitrate reductases.
作者信息
Blasco F, Guigliarelli B, Magalon A, Asso M, Giordano G, Rothery R A
机构信息
Laboratoire de Chimie Bactérienne, IBSM, CNRS, Marseille, France.
出版信息
Cell Mol Life Sci. 2001 Feb;58(2):179-93. doi: 10.1007/PL00000846.
Abstract
Under anaerobic conditions and in the presence of nitrate, the facultative anaerobe Escherichia coli synthesises an electron-transport chain comprising a primary dehydrogenase and the terminal membrane-bound nitrate reductase A (NarGHI). This review focuses on recent advances obtained on the structure and function of the three protein subunits of membrane-bound nitrate reductases. We discuss a global architecture for the Mo-bisMGD-containing subunit (NarG) and a coordination model for the four [Fe-S] centres of the electron-transfer subunit (NarH) and for the two b-type haems of the anchor subunit NarI.
摘要
在厌氧条件下且存在硝酸盐时，兼性厌氧菌大肠杆菌会合成一条电子传递链，该电子传递链由一种初级脱氢酶和末端膜结合硝酸盐还原酶A（NarGHI）组成。本综述聚焦于膜结合硝酸盐还原酶三个蛋白质亚基的结构与功能方面的最新进展。我们讨论了含钼双MGD亚基（NarG）的整体结构，以及电子传递亚基（NarH）的四个[Fe-S]中心和锚定亚基NarI的两个b型血红素的配位模型。
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