ArticleNature communications2015
ATP hydrolysis assists phosphate release and promotes reaction ordering in F1-ATPase.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 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
- Functional and structural characterization of FProtein science : a publication of the Protein Society · 2025Article
- Article
- Catalytic dwell oscillations complete the FCommunications chemistry · 2025Article
- Rotary properties of hybrid FiScience · 2023Article
- A novel approach to measure complex V ATP hydrolysis in frozen cell lysates and tissue homogenates.Life science alliance · 2023Article
- Angle-dependent rotation velocity consistent with ADP release in bacterial FFrontiers in molecular biosciences · 2023Article
- Scattering-based Light Microscopy: From Metal Nanoparticles to Single Proteins.Chemical reviews · 2021Review
- Article
- The 3 × 120° rotary mechanism ofProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Correlation between the numbers of rotation steps in the ATPase and proton-conducting domains of F- and V-ATPases.Biophysical reviews · 2020Article
- Efficiencies of molecular motors: a comprehensible overview.Biophysical reviews · 2020Review
- Rotary catalysis of bovine mitochondrial FProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Method to extract multiple states in FProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Single-molecule analysis reveals rotational substeps and chemo-mechanical coupling scheme ofThe Journal of biological chemistry · 2019Article
- Structure and dynamics of rotary VCellular and molecular life sciences : CMLS · 2018Review
- Deciphering Intrinsic Inter-subunit Couplings that Lead to Sequential Hydrolysis of FBiophysical journal · 2017Article
- Catalytic robustness and torque generation of the FBiophysical reviews · 2017Review
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
F1-ATPase (F1) is a rotary motor protein that can efficiently convert chemical energy to mechanical work of rotation via fine coordination of its conformational motions and reaction sequences. Compared with reactant binding and product release, the ATP hydrolysis has relatively little contributions to the torque and chemical energy generation. To scrutinize possible roles of ATP hydrolysis, we investigate the detailed statistics of the catalytic dwells from high-speed single wild-type F1 observations. Here we report a small rotation during the catalytic dwell triggered by the ATP hydrolysis that is indiscernible in previous studies. Moreover, we find in freely rotating F1 that ATP hydrolysis is followed by the release of inorganic phosphate with low synthesis rates. Finally, we propose functional roles of the ATP hydrolysis as a key to kinetically unlock the subsequent phosphate release and promote the correct reaction ordering.
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