Electron microscopy of the F1F0 ATP synthase: From structure to function

Electron microscopy of the F1F0 ATP synthase: From structure to function
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F1F0 ATP 合酶的电子显微镜:从结构到功能

DOI:
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发表时间:
1994
期刊:
Microscopy research and technique (Print)
影响因子:
--
通讯作者:
E. Gogol
E. Gogol
中科院分区:
--
文献类型:
--
作者:
E. Gogol

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1F0 ATP合成酶是一种大型多亚基复合物,它利用能量活性膜的质子梯度来合成ATP。虽然生物化学和遗传学方法已经表征了酶的组成并阐明了其机制和组装的许多细节,但电子显微镜在确定包括F1F0的许多亚基的排列方面一直是最重要的工具。高度合作的催化机制是紧密耦合到跨膜质子易位在一个单独的和相当遥远的部门的复杂。要理解这个复杂的过程及其控制,需要了解亚基相互作用,首先是它们之间的相对位置。电子显微镜已经提供了F1F0的大部分可用结构信息,并且低温电子显微镜的最新应用已经捕获了不同的功能相关构型,这些构型可能最终解决关于催化循环期间亚基重排的长期问题。© 1994 Wiley利斯公司
The 1F0 ATP synthase is the large multisubunit complex which uses the proton gradient of energetically active membranes to synthesize ATP. While biochemical and genetic approaches have characterized the composition of the enzyme and elucidated many details of its mechanism and assembly, electron microscopy has been the tool of primary importance in determining the arrangement of the many subunits which comprise the F1F0. The highly cooperative catalytic mechanism is tightly coupled to transmembrane proton translocation in a separate and rather distant sector of the complex. An understanding of this intricate process and its control requires an appreciation of subunit interactions, starting with their locations relative to one another. Electron microscopy has provided most of the available structural information on the F1F0, and recent applications of cryo‐electron microscopy have captured different functionally relevant configurations which may finally address longstanding questions about subunit rearrangement during the catalytic cycle. © 1994 Wiley‐Liss, Inc.
DOI: 10.1016/s0021-9258(18)92736-5
发表时间: 1991-07
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影响因子: --
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