Abstract
We experimentally show that biological molecular motor F_{1}-ATPase (F_{1}) implements an optimal rectification mechanism. The rectification mechanism hardly suppresses the synthesis of adenosine triphosphate by F_{1}, which is F_{1}'s physiological role, while inhibiting the unfavorable hydrolysis of adenosine triphosphate. This optimal rectification contrasts highly with that of a simple ratchet model, where the inhibition of the backward current is inevitably accompanied by the suppression of the forward current. Our detailed analysis of single-molecule trajectories demonstrates a novel but simple rectification mechanism of F_{1} with parallel landscapes and asymmetric transition rates.
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