We experimentally showed that biological molecular motor F$_1$-ATPase (F$_1$) implements an optimal rectification mechanism. F$_1$ hardly suppresses adenosine triphosphate (ATP) synthesis, which is the F$_1$'s physiological role while inhibiting unfavorable hydrolysis of ATP. This optimal rectification is a high contrast to a simple ratchet model, where the inhibition of the backward current is inevitably accompanied by the suppression of the forward current. The detailed analysis of single-molecule trajectories demonstrated a novel but simple rectification mechanism of F$_1$ with parallel landscapes and asymmetric transition rates.
Categories: physics.bio-ph