ArticleBiophysical journal2010
On the question of hydronium binding to ATP-synthase membrane rotors.
Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Decoding the Hot-Mitochondrion Paradox.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026Review
- Review
- Membrane plasticity facilitates recognition of the inhibitor oligomycin by the mitochondrial ATP synthase rotor.Biochimica et biophysica acta. Bioenergetics · 2018Article
- Predicted Structures of the Proton-Bound Membrane-Embedded Rotor Rings of the Saccharomyces cerevisiae and Escherichia coli ATP Synthases.The journal of physical chemistry. B · 2017Article
- Article
- Structure and mechanism of the ATP synthase membrane motor inferred from quantitative integrative modeling.The Journal of general physiology · 2016Article
- On the principle of ion selectivity in Na+/H+-coupled membrane proteins: experimental and theoretical studies of an ATP synthase rotor.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- High-resolution structure and mechanism of an F/V-hybrid rotor ring in a Na⁺-coupled ATP synthase.Nature communications · 2014Article
- The c-ring ion binding site of the ATP synthase from Bacillus pseudofirmus OF4 is adapted to alkaliphilic lifestyle.Molecular microbiology · 2014Article
- Mussel and mammalian ATP synthase share the same bioenergetic cost of ATP.Journal of bioenergetics and biomembranes · 2013Article
- A new type of Na(+)-driven ATP synthase membrane rotor with a two-carboxylate ion-coupling motif.PLoS biology · 2013Article
- A c subunit with four transmembrane helices and one ion (Na+)-binding site in an archaeal ATP synthase: implications for c ring function and structure.The Journal of biological chemistry · 2012Article
- Structure of the c(10) ring of the yeast mitochondrial ATP synthase in the open conformation.Nature structural & molecular biology · 2012Article
- Promiscuous archaeal ATP synthase concurrently coupled to Na+ and H+ translocation.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Structure-function relationships in membrane segment 6 of the yeast plasma membrane Pma1 H(+)-ATPase.Biochimica et biophysica acta · 2011Article
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Authors and funding
3 authors.
Funding
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Abstract
A recently determined atomic structure of an H(+)-coupled ATP-synthase membrane rotor has revived the long-standing question of whether protons may be bound to these structures in the form of a hydronium ion. Using both classical and quantum-mechanical simulations, we show that this notion is implausible. Ab initio molecular dynamics simulations of the binding site demonstrate that the putative H(3)O(+) deprotonates within femtoseconds. The bound proton is thus transferred irreversibly to the carboxylate side chain found in the ion-binding sites of all ATP-synthase rotors. This result is consistent with classical simulations of the rotor in a phospholipid membrane, on the 100-nanosecond timescale. These simulations show that the hydrogen-bond network seen in the crystal structure is incompatible with a bound hydronium. The observed coordination geometry is shown to correspond instead to a protonated carboxylate and a bound water molecule. In conclusion, this study underscores the notion that binding and transient storage of protons in the membrane rotors of ATP synthases occur through a common chemical mechanism, namely carboxylate protonation.
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