ArticleThe Journal of biological chemistry2014
Robustness of the rotary catalysis mechanism of F1-ATPase.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 11 citations in OpenAlex.
- High-throughput mutational analysis 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
- Rotary properties of hybrid FiScience · 2023Article
- Application of the fluctuation theorem to motor proteins: from FBiophysical reviews · 2018Review
- The FPhotosynthesis research · 2017Review
- Catalytic robustness and torque generation of the FBiophysical reviews · 2017Review
- Development of Potent Antiviral Drugs Inspired by Viral Hexameric DNA-Packaging Motors with Revolving Mechanism.Journal of virology · 2016Review
- Discovery of a new method for potent drug development using power function of stoichiometry of homomeric biocomplexes or biological nanomotors.Expert opinion on drug delivery · 2016Article
- A mechano-chemiosmotic model for the coupling of electron and proton transfer to ATP synthesis in energy-transforming membranes: a personal perspective.Photosynthesis research · 2015Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
F1-ATPase (F1) is the rotary motor protein fueled by ATP hydrolysis. Previous studies have suggested that three charged residues are indispensable for catalysis of F1 as follows: the P-loop lysine in the phosphate-binding loop, GXXXXGK(T/S); a glutamic acid that activates water molecules for nucleophilic attack on the γ-phosphate of ATP (general base); and an arginine directly contacting the γ-phosphate (arginine finger). These residues are well conserved among P-loop NTPases. In this study, we investigated the role of these charged residues in catalysis and torque generation by analyzing alanine-substituted mutants in the single-molecule rotation assay. Surprisingly, all mutants continuously drove rotary motion, even though the rotational velocity was at least 100,000 times slower than that of wild type. Thus, although these charged residues contribute to highly efficient catalysis, they are not indispensable to chemo-mechanical energy coupling, and the rotary catalysis mechanism of F1 is far more robust than previously thought.
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