Electric Field Driven Torque in ATP Synthase

被引:22
|
作者
Miller, John H., Jr. [1 ,2 ]
Rajapakshe, Kimal I. [1 ,2 ,3 ]
Infante, Hans L. [1 ,2 ]
Claycomb, James R. [1 ,2 ,4 ]
机构
[1] Univ Houston, Dept Phys, Houston, TX 77204 USA
[2] Univ Houston, Texas Ctr Superconduct, Houston, TX USA
[3] Baylor Coll Med, Dept Mol & Cellular Biol, Houston, TX 77030 USA
[4] Houston Baptist Univ, Dept Math & Phys, Houston, TX USA
来源
PLOS ONE | 2013年 / 8卷 / 09期
基金
美国国家卫生研究院;
关键词
PROTON TRANSPORT; PATHOGENIC MECHANISM; AQUEOUS ACCESS; MUTATIONS; CANCER; SUBUNIT; VOLTAGE; T8993G; MOTOR; GENERATION;
D O I
10.1371/journal.pone.0074978
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
F-O-ATP synthase (F-O) is a rotary motor that converts potential energy from ions, usually protons, moving from high- to low-potential sides of a membrane into torque and rotary motion. Here we propose a mechanism whereby electric fields emanating from the proton entry and exit channels act on asymmetric charge distributions in the c-ring, due to protonated and deprotonated sites, and drive it to rotate. The model predicts a scaling between time-averaged torque and proton motive force, which can be hindered by mutations that adversely affect the channels. The torque created by the c-ring of F-O drives the gamma-subunit to rotate within the ATP-producing complex (F-1) overcoming, with the aid of thermal fluctuations, an opposing torque that rises and falls with angular position. Using the analogy with thermal Brownian motion of a particle in a tilted washboard potential, we compute ATP production rates vs. proton motive force. The latter shows a minimum, needed to drive ATP production, which scales inversely with the number of proton binding sites on the c-ring.
引用
收藏
页数:9
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