von Ballmoos Christoph, Wiedenmann Alexander, Dimroth Peter
Department of Biochemistry and Biophysics, Arrhenius Laboratories for Natural Sciences, Stockholm University, Stockholm, Sweden.
Annu Rev Biochem. 2009;78:649-72. doi: 10.1146/annurev.biochem.78.081307.104803.
The majority of cellular energy in the form of adenosine triphosphate (ATP) is synthesized by the ubiquitous F(1)F(0) ATP synthase. Power for ATP synthesis derives from an electrochemical proton (or Na(+)) gradient, which drives rotation of membranous F(0) motor components. Efficient rotation not only requires a significant driving force (DeltamuH(+)), consisting of membrane potential (Deltapsi) and proton concentration gradient (DeltapH), but also a high proton concentration at the source P side. In vivo this is maintained by dynamic proton movements across and along the surface of the membrane. The torque-generating unit consists of the interface of the rotating c ring and the stator a subunit. Ion translocation through this unit involves a sophisticated interplay between the c-ring binding sites, the stator arginine, and the coupling ions on both sides of the membrane. c-ring rotation is transmitted to the eccentric shaft gamma-subunit to elicit conformational changes in the catalytic sites of F(1), leading to ATP synthesis.
大多数以三磷酸腺苷（ATP）形式存在的细胞能量是由普遍存在的F(1)F(0) ATP合酶合成的。ATP合成的动力来自电化学质子（或Na(+)）梯度，该梯度驱动膜性F(0) 马达组件的旋转。高效旋转不仅需要由膜电位（Δψ）和质子浓度梯度（ΔpH）组成的显著驱动力（ΔμH(+)），还需要在源P侧有高质子浓度。在体内，这是通过质子在膜表面的动态跨膜运动和沿膜表面的运动来维持的。扭矩产生单元由旋转的c环和定子a亚基的界面组成。离子通过该单元的转运涉及c环结合位点、定子精氨酸和膜两侧耦合离子之间复杂的相互作用。c环的旋转传递到偏心轴γ亚基，以引发F(1)催化位点的构象变化，从而导致ATP合成。
