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• W1987859844 startingPage "16468" @default.
• W1987859844 abstract "Significance F 1 -ATPase is the catalytic domain of F o F 1 -ATP synthase, the rotary molecular motor at the core of the energy transduction machinery in all of life. We use atomistic molecular dynamics simulations to study a key event in its catalytic cycle, the release of inorganic phosphate (P i ) produced by the hydrolysis of ATP. We determine the timing, kinetics, and molecular mechanism of P i release and clarify its role in torque generation. We also obtain an atomically detailed structure of a crystallographically unresolved intermediate formed after the 40° substep. Our results help reconcile conflicting interpretations of earlier biochemical, crystallographic, and single-molecule studies; shed light on the functional requirements of efficient ATP synthesis; and establish connections to other motors such as myosin." @default.
• W1987859844 created "2016-06-24" @default.
• W1987859844 creator A5054735430 @default.
• W1987859844 creator A5059945365 @default.
• W1987859844 date "2013-09-23" @default.
• W1987859844 modified "2023-10-16" @default.
• W1987859844 title "Phosphate release coupled to rotary motion of F ₁ -ATPase" @default.
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• W1987859844 doi "https://doi.org/10.1073/pnas.1305497110" @default.
• W1987859844 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3799341" @default.
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• W1987859844 hasPublicationYear "2013" @default.
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