ArticleBiophysical journal2004
ATP hydrolysis in the betaTP and betaDP catalytic sites of F1-ATPase.
Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
- A minimal chemo-mechanical Markov model for rotary catalysis of FNature communications · 2026Article
- The distortion-push mechanism for the γ subunit rotation in FProceedings of the National Academy of Sciences of the United States of America · 2025Article
- The molecular mechanism of ATP synthase constrains the evolutionary landscape of chemiosmosis.Biophysical journal · 2025Review
- Rotary properties of hybrid FiScience · 2023Article
- FFrontiers in microbiology · 2022Review
- Rotary catalysis of bovine mitochondrial FProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Catalytic robustness and torque generation of the FBiophysical reviews · 2017Review
- Theory for rates, equilibrium constants, and Brønsted slopes in F1-ATPase single molecule imaging experiments.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Kinesin Motor Enzymology: Chemistry, Structure, and Physics of Nanoscale Molecular Machines.Biophysical reviews · 2015Article
- Torque transmission mechanism via DELSEED loop of F1-ATPase.Biophysical journal · 2015Article
- Mechanism of the αβ conformational change in F1-ATPase after ATP hydrolysis: free-energy simulations.Biophysical journal · 2015Article
- Robustness of the rotary catalysis mechanism of F1-ATPase.The Journal of biological chemistry · 2014Article
- Timing of inorganic phosphate release modulates the catalytic activity of ATP-driven rotary motor protein.Nature communications · 2014Article
- Anatomy of F1-ATPase powered rotation.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Single-molecule analysis of the rotation of F₁-ATPase under high hydrostatic pressure.Biophysical journal · 2013Article
- Quantum and classical dynamics simulations of ATP hydrolysis in solution.Journal of chemical theory and computation · 2012Article
- Domain motion of individual F1-ATPase β-subunits during unbiased molecular dynamics simulations.The journal of physical chemistry. A · 2011Article
- Torsional elasticity and energetics of F1-ATPase.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Double-lock ratchet mechanism revealing the role of alphaSER-344 in FoF1 ATP synthase.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- The glmS ribozyme: use of a small molecule coenzyme by a gene-regulatory RNA.Quarterly reviews of biophysics · 2010Review
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3 authors.
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Abstract
The enzyme F1-adenosine triphosphatase (ATPase) is a molecular motor that converts the chemical energy stored in the molecule adenosine triphosphate (ATP) into mechanical rotation of its gamma-subunit. During steady-state catalysis, the three catalytic sites of F1 operate in a cooperative fashion such that at every instant each site is in a different conformation corresponding to a different stage along the catalytic cycle. Notwithstanding a large amount of biochemical and, recently, structural data, we still lack an understanding of how ATP hydrolysis in F1 is coupled to mechanical motion and how the catalytic sites achieve cooperativity during rotatory catalysis. In this publication, we report combined quantum mechanical/molecular mechanical simulations of ATP hydrolysis in the betaTP and betaDP catalytic sites of F1-ATPase. Our simulations reveal a dramatic change in the reaction energetics from strongly endothermic in betaTP to approximately equienergetic in betaDP. The simulations identify the responsible protein residues, the arginine finger alphaR373 being the most important one. Similar to our earlier study of betaTP, we find a multicenter proton relay mechanism to be the energetically most favorable hydrolysis pathway. The results elucidate how cooperativity between catalytic sites might be achieved by this remarkable molecular motor.
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