2014
DOI: 10.1073/pnas.1419486111
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Trapping the ATP binding state leads to a detailed understanding of the F 1 -ATPase mechanism

Abstract: The rotary motor enzyme F o F 1 -ATP synthase uses the protonmotive force across a membrane to synthesize ATP from ADP and P i (H 2 PO 4 − ) under cellular conditions that favor the hydrolysis reaction by a factor of 2 × 10 5 . This remarkable ability to drive a reaction away from equilibrium by harnessing an external force differentiates it from an ordinary enzyme, which increases the rate of reaction without shifting the equilibrium. Hydrolysis takes place in the neighborhood of one conformation of the catal… Show more

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Cited by 55 publications
(84 citation statements)
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“…According to the established catalytic scheme of bacterial F 1 , binding of ATP to F 1 induces the stepping rotation of the γ from 0°to 80°and release of P i from F 1 does so from 80°to 120°(4-6). Similar stepwise rotation of the γ subunit was simulated for bovine F 1 (25,26). Therefore, state III defined in this study corresponds to F 1 in the state waiting for ATP binding (pre-ATP-binding state) and state II corresponds to F 1 in the state waiting for P i release (pre-P i -release state).…”
Section: Discussionmentioning
confidence: 82%
“…According to the established catalytic scheme of bacterial F 1 , binding of ATP to F 1 induces the stepping rotation of the γ from 0°to 80°and release of P i from F 1 does so from 80°to 120°(4-6). Similar stepwise rotation of the γ subunit was simulated for bovine F 1 (25,26). Therefore, state III defined in this study corresponds to F 1 in the state waiting for ATP binding (pre-ATP-binding state) and state II corresponds to F 1 in the state waiting for P i release (pre-P i -release state).…”
Section: Discussionmentioning
confidence: 82%
“…Molecular dynamics (MD) simulations (14)(15)(16) can help interpret such data in a dynamic context. However, there is scant information on how the conformation of F o F 1 is affected by internal and external forces while working under physiological conditions, where ATP/ADP interconversion is coupled with transmembrane proton transport in the presence of proton-motive force (PMF).…”
mentioning
confidence: 99%
“…Although the crystal structures of the α 3 β 3 γ-complex differ from each other in terms of their nucleotide binding states and detailed configurations of the residues, their global structures are similar to the first crystal structure (19), which leaves the structure of the ATP waiting form unresolved. Closing this gap in the conformational cycle will deepen our understanding of the coupling between chemical reactions, α 3 β 3 -conformations, conformations, and rotary angles, not least by providing critical input into the theoretical modeling of F 1 (20)(21)(22)(23)(24)(25)(26).…”
mentioning
confidence: 99%