THE REGULATION OF CATALYSIS IN ATP SYNTHASE

被引：92

作者：

WALKER, JE

机构：

[1] Medical Research Council Laboratory of Molecular Biology, Cambridge

来源：

CURRENT OPINION IN STRUCTURAL BIOLOGY | 1994年 / 4卷 / 06期

关键词：

D O I：

10.1016/0959-440X(94)90274-7

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

ATP synthase is regulated so as to prevent futile hydrolysis of ATP when the transmembrane proton electrochemical gradient, Delta mu(H)(+), falls. Mitochondria and chloroplasts have different mechanisms for inhibition of ATP synthase: by binding an inhibitor protein, and by stabilization of the ADP-inhibited state by making an intramolecular disulphide bond, respectively. The recently determined structure of bovine F-1-ATPase is locked in a conformation that probably represents the ADP-inhibited state of the enzyme.

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页码：912 / 918

页数：7

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