Abstract
Single molecule observations of the F1 sector of the E. coli ATP synthase were made in Vmax conditions with minimal load. The enzyme rotates through continuous cycles of catalytic dwells (pauses lasting ∼0.2 ms) and 120° rotation steps (∼0.6 ms in duration). We previously established that the rate limiting transition state step occurs during the catalytic dwell just prior to the initiation of the 120° rotation. Here we use the phytopolyphenol stilbenoid inhibitor, piceatannol, which binds to a pocket formed by contributions from α and β stator subunits and the carboxyl terminal region of the rotor γ subunit.
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