Efficiently Driving F_{1} Molecular Motor in Experiment by Suppressing Nonequilibrium Variation

Abstract

F_{1}-ATPase (F_{1}) is central to cellular energy transduction. Forcibly rotated by another motor F_{o}, F_{1} catalyzes adenosine triphosphate (ATP) synthesis by converting mechanical work into chemical free energy stored in the molecule ATP. The details of how F_{o} drives F_{1} are not fully understood

however, evaluating efficient ways to rotate F_{1} could provide fruitful insights into this driving since there is a selective pressure to improve efficiency. Here, we show that rotating F_{1} with an angle clamp is significantly more efficient than a constant torque. Our experiments, combined with theory and simulation, indicate that the angle clamp significantly suppresses the nonequilibrium variation that contributes to the futile dissipation of input work. This record is sourced from MEDLINE/PubMed, a database of the U.S. National Library of Medicine