ATP合酶的旋转结合变化机制。
The rotary binding change mechanism of ATP synthases.
作者信息
Cross R L
机构信息
Department of Biochemistry and Molecular Biology, State University of New York, Health Science Center, Syracuse, NY 13210, USA.
出版信息
Biochim Biophys Acta. 2000 May 31;1458(2-3):270-5. doi: 10.1016/s0005-2728(00)00079-7.
The F(0)F(1) ATP synthase functions as a rotary motor where subunit rotation driven by a current of protons flowing through F(0) drives the binding changes in F(1) that are required for net ATP synthesis. Recent work that has led to the identification of components of the rotor and stator is reviewed. In addition, a model is proposed to describe the transmission of energy from four proton transport steps to the synthesis of one ATP. Finally, some of the requirements for efficient energy coupling by a rotary binding change mechanism are considered.
F(0)F(1) ATP合酶起着旋转马达的作用，其中由流经F(0)的质子流驱动的亚基旋转推动F(1)中发生结合变化，这是净ATP合成所必需的。本文综述了近期有关转子和定子组件鉴定的研究工作。此外，还提出了一个模型来描述从四个质子传输步骤到一个ATP合成的能量传递。最后，考虑了通过旋转结合变化机制实现高效能量耦合的一些要求。
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