ArticleThe Journal of biological chemistry2015
Fo-driven Rotation in the ATP Synthase Direction against the Force of F1 ATPase in the FoF1 ATP Synthase.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
12 citing papers in PubMed.
- Catalytic dwell oscillations complete the FCommunications chemistry · 2025Article
- Mechanism of proton-powered c-ring rotation in a mitochondrial ATP synthase.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Mutational analysis of a conserved positive charge in the c-ring of E. coli ATP synthase.Biochimica et biophysica acta. Bioenergetics · 2023Article
- Beyond binding change: the molecular mechanism of ATP hydrolysis by FFrontiers in chemistry · 2023Article
- Direct observation of stepping rotation of V-ATPase reveals rigid component in coupling between VProceedings of the National Academy of Sciences of the United States of America · 2022Article
- FFrontiers in microbiology · 2022Review
- pH-dependent 11° FeLife · 2021Article
- Structural Asymmetry and Kinetic Limping of Single Rotary F-ATP Synthases.Molecules (Basel, Switzerland) · 2019Review
- Elastic coupling power stroke mechanism of the FProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Protonation-dependent stepped rotation of the F-type ATP synthase c-ring observed by single-molecule measurements.The Journal of biological chemistry · 2017Article
- Nanodiscs in Membrane Biochemistry and Biophysics.Chemical reviews · 2017Review
- The Mitochondrial Permeability Transition Pore: Channel Formation by F-ATP Synthase, Integration in Signal Transduction, and Role in Pathophysiology.Physiological reviews · 2015Review
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Living organisms rely on the FoF1 ATP synthase to maintain the non-equilibrium chemical gradient of ATP to ADP and phosphate that provides the primary energy source for cellular processes. How the Fo motor uses a transmembrane electrochemical ion gradient to create clockwise torque that overcomes F1 ATPase-driven counterclockwise torque at high ATP is a major unresolved question. Using single FoF1 molecules embedded in lipid bilayer nanodiscs, we now report the observation of Fo-dependent rotation of the c10 ring in the ATP synthase (clockwise) direction against the counterclockwise force of ATPase-driven rotation that occurs upon formation of a leash with Fo stator subunit a. Mutational studies indicate that the leash is important for ATP synthase activity and support a mechanism in which residues aGlu-196 and cArg-50 participate in the cytoplasmic proton half-channel to promote leash formation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.