Key result
Forced rotations reveal negligible internal dissipation of the F1-motor during ATP synthesis.
Why the study?
The mechanical-to-chemical free-energy transduction by the F1-ATPase motor during ATP synthesis under forced rotation was not quantitatively determined.
The study demonstrates that the F1-motor has negligible internal dissipation during ATP synthesis driven by forced rotations.
F o F 1 -ATP synthase is a factory for synthesizing ATP in virtually all cells. Its core machinery is the subcomplex F 1 -motor (F 1 -ATPase) and performs the reversible mechanochemical coupling. The isolated F 1 -motor hydrolyzes ATP, which is accompanied by unidirectional rotation of its central . When a strong opposing torque is imposed, the -shaft rotates in the opposite direction and drives the F 1 -motor to synthesize ATP. This mechanical-to-chemical free-energy transduction is the final and central step of the multistep cellular ATP-synthetic pathway. Here, we determined the amount of mechanical work exploited by the F 1 -motor to synthesize an ATP molecule during forced rotations using a methodology combining a nonequilibrium theory and single molecule measurements of responses to external torque. We found that the internal dissipation of the motor is negligible even during rotations far from a quasistatic process.
No takes yet. Share an insight, caveat, or question.
A 2015 study studied this question. Forced rotations using external torque was evaluated on Amount of mechanical work exploited by the F1-motor to synthesize an ATP molecule. Internal dissipation of the F1-motor during ATP synthesis is negligible even during forced rotations far from a quasistatic process.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: