ATP合酶的旋转机制。
The rotary mechanism of the ATP synthase.
作者信息
Nakamoto Robert K, Baylis Scanlon Joanne A, Al-Shawi Marwan K
机构信息
Department of Molecular Physiology and Biological Physics, University of Virginia, P.O. Box 800736, Charlottesville, VA 22908-0736, USA.
出版信息
Arch Biochem Biophys. 2008 Aug 1;476(1):43-50. doi: 10.1016/j.abb.2008.05.004. Epub 2008 May 20.
Abstract
The F0F1 ATP synthase is a large complex of at least 22 subunits, more than half of which are in the membranous F0 sector. This nearly ubiquitous transporter is responsible for the majority of ATP synthesis in oxidative and photo-phosphorylation, and its overall structure and mechanism have remained conserved throughout evolution. Most examples utilize the proton motive force to drive ATP synthesis except for a few bacteria, which use a sodium motive force. A remarkable feature of the complex is the rotary movement of an assembly of subunits that plays essential roles in both transport and catalytic mechanisms. This review addresses the role of rotation in catalysis of ATP synthesis/hydrolysis and the transport of protons or sodium.
摘要
F0F1型ATP合酶是一种由至少22个亚基组成的大型复合体，其中一半以上位于膜状的F0部分。这种几乎无处不在的转运体负责氧化磷酸化和光合磷酸化过程中大部分的ATP合成，其整体结构和机制在整个进化过程中一直保持保守。除了少数利用钠动力的细菌外，大多数例子都利用质子动力来驱动ATP合成。该复合体的一个显著特征是亚基组件的旋转运动，这在转运和催化机制中都起着至关重要的作用。本文综述了旋转在ATP合成/水解催化以及质子或钠转运中的作用。
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