Abstract
Understanding how F1Fo-ATP synthase (F-ATP synthase) synthesizes ATP from ADP and phosphate is essential for understanding how life on the earth converts and utilizes energy. Studies on isolated F1-ATPase, the soluble sector of F-ATP synthase, which catalyzes ATP hydrolysis in aqueous solution, provide promising insights about the mechanism of F-ATP synthase. A paradigm named rotary catalysis, or binding-change mechanism, has been established to explain ATP hydrolysis mechanism of F1-ATPase, where rotation of the γ-subunit, conformational transition of the β-subunits and nucleotide exchange at catalytic sites are delicately coordinated to maintain a high chemo-mechanical coupling efficiency.
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