ArticleProceedings of the National Academy of Sciences of the United States of America2014
Anatomy of F1-ATPase powered rotation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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Who cites it
58 citing papers in PubMed.
- The lower γ region supports forward rotation in the latter half of the 80° substep of FProtein science : a publication of the Protein Society · 2026Article
- The molecular mechanism of ATP synthase constrains the evolutionary landscape of chemiosmosis.Biophysical journal · 2025Review
- The ATPase asymmetry: Novel computational insight into coupling diverse FBiophysical journal · 2025Article
- Catalytic dwell oscillations complete the FCommunications chemistry · 2025Article
- The molecular structure of an axle-less FbioRxiv : the preprint server for biology · 2024Article
- Conformational ensemble of yeast ATP synthase at low pH reveals unique intermediates and plasticity in FNature structural & molecular biology · 2024Article
- Eukaryotic yeast VFrontiers in molecular biosciences · 2024Article
- Elucidating Events within the Black Box of Enzyme Catalysis in Energy Metabolism: Insights into the Molecular Mechanism of ATP Hydrolysis by FBiomolecules · 2023Article
- FBiophysical journal · 2023Article
- Waiting Time Distributions in Hybrid Models of Motor-Bead Assays: A Concept and Tool for Inference.International journal of molecular sciences · 2023Article
- Molecular mechanism on forcible ejection of ATPase inhibitory factor 1 from mitochondrial ATP synthase.Nature communications · 2023Article
- Light, Water, and Melatonin: The Synergistic Regulation of Phase Separation in Dementia.International journal of molecular sciences · 2023Review
- Direct identification of the rotary angle of ATP cleavage in FBiophysical journal · 2023Article
- Structural Elements Involved in ATP Hydrolysis Inhibition and ATP Synthesis of Tuberculosis and Nontuberculous Mycobacterial F-ATP Synthase Decipher New Targets for Inhibitors.Antimicrobial agents and chemotherapy · 2022Article
- 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
- Structure of ATP synthase under strain during catalysis.Nature communications · 2022Article
- Assembly and Analysis of Cell-Scale Membrane Envelopes.Journal of chemical information and modeling · 2022Article
- Modulation of the HFrontiers in molecular biosciences · 2022Review
- FFrontiers in microbiology · 2022Review
- Delineating specific regions of N- terminal domain of T3SS ATPase YsaN ofFrontiers in molecular biosciences · 2022Article
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5 authors.
Funding
Abstract
F1-ATPase, the catalytic complex of the ATP synthase, is a molecular motor that can consume ATP to drive rotation of the γ-subunit inside the ring of three αβ-subunit heterodimers in 120° power strokes. To elucidate the mechanism of ATPase-powered rotation, we determined the angular velocity as a function of rotational position from single-molecule data collected at 200,000 frames per second with unprecedented signal-to-noise. Power stroke rotation is more complex than previously understood. This paper reports the unexpected discovery that a series of angular accelerations and decelerations occur during the power stroke. The decreases in angular velocity that occurred with the lower-affinity substrate ITP, which could not be explained by an increase in substrate-binding dwells, provides direct evidence that rotation depends on substrate binding affinity. The presence of elevated ADP concentrations not only increased dwells at 35° from the catalytic dwell consistent with competitive product inhibition but also decreased the angular velocity from 85° to 120°, indicating that ADP can remain bound to the catalytic site where product release occurs for the duration of the power stroke. The angular velocity profile also supports a model in which rotation is powered by Van der Waals repulsive forces during the final 85° of rotation, consistent with a transition from F1 structures 2HLD1 and 1H8E (Protein Data Bank).
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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.