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ATP合酶中催化作用的调节

The regulation of catalysis in ATP synthase.

作者信息

Walker J E

机构信息

Medical Research Council Laboratory of Molecular Biology, Cambridge, UK.

出版信息

Curr Opin Struct Biol. 1994 Dec;4(6):912-8. doi: 10.1016/0959-440x(94)90274-7.

DOI:10.1016/0959-440x(94)90274-7
PMID:7712295
Abstract

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 F1-ATPase is locked in a conformation that probably represents the ADP-inhibited state of the enzyme.

摘要

当跨膜质子电化学梯度ΔμH⁺下降时,ATP合酶会受到调节,以防止ATP的无效水解。线粒体和叶绿体对ATP合酶的抑制机制不同:分别是通过结合一种抑制蛋白,以及通过形成分子内二硫键来稳定ADP抑制状态。最近确定的牛F1-ATP酶的结构被锁定在一种构象中,这种构象可能代表了该酶的ADP抑制状态。

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