ArticleNature communications2014
Timing of inorganic phosphate release modulates the catalytic activity of ATP-driven rotary motor protein.
Article in Nature communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 52 citations in OpenAlex.
- High-throughput mutational analysis of FProtein science : a publication of the Protein Society · 2026Article
- Nucleotide Exchange Mechanism Involving Angle-Dependent Rate Constants Extracted from F1-ATPase Single-Molecule Rotation Trajectories.The journal of physical chemistry. B · 2026Article
- Catalytic dwell oscillations complete the FCommunications chemistry · 2025Article
- Mechanism of ATP hydrolysis dependent rotation of bacterial ATP synthase.Nature communications · 2023Article
- Molecular mechanism on forcible ejection of ATPase inhibitory factor 1 from mitochondrial ATP synthase.Nature communications · 2023Article
- Direct identification of the rotary angle of ATP cleavage in FBiophysical journal · 2023Article
- Cryo-EM analysis of V/A-ATPase intermediates reveals the transition of the ground-state structure to steady-state structures by sequential ATP binding.The Journal of biological chemistry · 2023Article
- Structural snapshots of V/A-ATPase reveal the rotary catalytic mechanism of rotary ATPases.Nature communications · 2022Article
- FFrontiers in microbiology · 2022Review
- 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
- The structure of the catalytic domain of the ATP synthase fromProceedings of the National Academy of Sciences of the United States of America · 2019Article
- Identification of two segments of the γ subunit of ATP synthase responsible for the different affinities of the catalytic nucleotide-binding sites.The Journal of biological chemistry · 2019Article
- Essential Role of the ε Subunit for Reversible Chemo-Mechanical Coupling in FBiophysical journal · 2018Article
- Deciphering Intrinsic Inter-subunit Couplings that Lead to Sequential Hydrolysis of FBiophysical journal · 2017Article
- The uniqueness of subunit α of mycobacterial F-ATP synthases: An evolutionary variant for niche adaptation.The Journal of biological chemistry · 2017Article
- Dynamic mechanisms driving conformational conversions of the β and ε subunits involved in rotational catalysis of FProceedings of the Japan Academy. Series B, Physical and biological sciences · 2017Review
- Crystal structures of the ATP-binding and ADP-release dwells of the VNature communications · 2016Article
- Theory of single-molecule controlled rotation experiments, predictions, tests, and comparison with stalling experiments in F1-ATPase.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- A gating mechanism for Pi release governs the mRNA unwinding by eIF4AI during translation initiation.Nucleic acids research · 2015Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
F1-ATPase is a rotary motor protein driven by ATP hydrolysis. The rotary motion of F1-ATPase is tightly coupled to catalysis, in which the catalytic sites strictly obey the reaction sequences at the resolution of elementary reaction steps. This fine coordination of the reaction scheme is thought to be important to achieve extremely high chemomechanical coupling efficiency and reversibility, which is the prominent feature of F1-ATPase among molecular motor proteins. In this study, we intentionally change the reaction scheme by using single-molecule manipulation, and we examine the resulting effect on the rotary motion of F1-ATPase. When the sequence of the products released, that is, ADP and inorganic phosphate, is switched, we find that F1 frequently stops rotating for a long time, which corresponds to inactivation of catalysis. This inactive state presents MgADP inhibition, and thus, we find that an improper reaction sequence of F1-ATPase catalysis induces MgADP inhibition.
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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.