We experimentally show that biological molecular motor F1-ATPase (F1) implements an optimal rectification mechanism. The rectification mechanism hardly suppresses the synthesis of adenosine triphosphate by F1, which is F1'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 F1 with parallel landscapes and asymmetric transition rates.
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