1. Electric Field Driven Torque in ATP Synthase.
- Author
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Miller Jr, John H., Rajapakshe, Kimal I., Infante, Hans L., and Claycomb, James R.
- Subjects
ADENOSINE triphosphatase ,ELECTRIC fields ,TORQUE ,ELECTRIC charge ,BROWNIAN motion ,BINDING sites ,GENETIC mutation - Abstract
F
O -ATP synthase (FO ) 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 FO drives the γ-subunit to rotate within the ATP-producing complex (F1 ) 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. [ABSTRACT FROM AUTHOR]- Published
- 2013
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