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- W2783998548 abstract "F1-ATPase is a rotary motor protein driven by ATP hydrolysis. Among molecular motors, F1 exhibits unique high reversibility in chemo-mechanical coupling, synthesizing ATP from ADP and inorganic phosphate upon forcible rotor reversal. The ε subunit enhances ATP synthesis coupling efficiency to > 70% upon rotation reversal. However, the detailed mechanism has remained elusive. In this study, we performed stall-and-release experiments to elucidate how the ε subunit modulates ATP association/dissociation and hydrolysis/synthesis process kinetics and thermodynamics, key reaction steps for efficient ATP synthesis. The ε subunit significantly accelerated the rates of ATP dissociation and synthesis by two- to fivefold, whereas those of ATP binding and hydrolysis were not enhanced. Numerical analysis based on the determined kinetic parameters quantitatively reproduced previous findings of two- to fivefold coupling efficiency improvement by the ε subunit at the condition exhibiting the maximum ATP synthesis activity, a physiological role of F1-ATPase. Furthermore, fundamentally similar results were obtained upon ε subunit C-terminal domain truncation, suggesting that the N-terminal domain is responsible for the rate enhancement." @default.
- W2783998548 created "2018-01-26" @default.
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- W2783998548 date "2018-01-01" @default.
- W2783998548 modified "2023-10-18" @default.
- W2783998548 title "Essential Role of the ε Subunit for Reversible Chemo-Mechanical Coupling in F1-ATPase" @default.
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- W2783998548 doi "https://doi.org/10.1016/j.bpj.2017.11.004" @default.
- W2783998548 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5773760" @default.
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- W2783998548 hasPublicationYear "2018" @default.
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