ArticleNature chemical biology2010
Microscopic rotary mechanism of ion translocation in the F(o) complex of ATP synthases.
Article in Nature chemical biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
79 citing papers in PubMed, 150 citations in OpenAlex.
- Secondary metabolites fromRSC advances · 2026Article
- Structure of ATP synthase from an early photosynthetic bacteriumProceedings of the National Academy of Sciences of the United States of America · 2025Article
- The ATPase asymmetry: Novel computational insight into coupling diverse FBiophysical journal · 2025Article
- Purification and Reconstitution of Ilyobacter tartaricus ATP Synthase.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Mechanism of proton-powered c-ring rotation in a mitochondrial ATP synthase.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- FBiophysical journal · 2023Article
- Mutational analysis of a conserved positive charge in the c-ring of E. coli ATP synthase.Biochimica et biophysica acta. Bioenergetics · 2023Article
- Top-Down Identification and Sequence Analysis of Small Membrane Proteins Using MALDI-MS/MS.Journal of the American Society for Mass Spectrometry · 2022Article
- ATP synthase FCellular and molecular life sciences : CMLS · 2022Review
- Determinants of Directionality and Efficiency of the ATP Synthase FThe journal of physical chemistry letters · 2022Article
- Binding properties of the anti-TB drugs bedaquiline and TBAJ-876 to a mycobacterial F-ATP synthase.Current research in structural biology · 2022Article
- FFrontiers in microbiology · 2022Review
- Rotational Mechanism of FFrontiers in microbiology · 2022Review
- ATP Synthase KFunction (Oxford, England) · 2022Article
- pH-dependent 11° FeLife · 2021Article
- Rotor subunits adaptations in ATP synthases from photosynthetic organisms.Biochemical Society transactions · 2021Review
- Molecular and Supramolecular Structure of the Mitochondrial Oxidative Phosphorylation System: Implications for Pathology.Life (Basel, Switzerland) · 2021Review
- Article
- The 3 × 120° rotary mechanism ofProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Case Report: Identification of a Novel Variant (m.8909T>C) of Human MitochondrialLife (Basel, Switzerland) · 2020Article
19 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The microscopic mechanism of coupled c-ring rotation and ion translocation in F(1)F(o)-ATP synthases is unknown. Here we present conclusive evidence supporting the notion that the ability of c-rings to rotate within the F(o) complex derives from the interplay between the ion-binding sites and their nonhomogenous microenvironment. This evidence rests on three atomic structures of the c(15) rotor from crystals grown at low pH, soaked at high pH and, after N,N'-dicyclohexylcarbodiimide (DCCD) modification, resolved at 1.8, 3.0 and 2.2 Å, respectively. Alongside a quantitative DCCD-labeling assay and free-energy molecular dynamics calculations, these data demonstrate how the thermodynamic stability of the so-called proton-locked state is maximized by the lipid membrane. By contrast, a hydrophilic environment at the a-subunit-c-ring interface appears to unlock the binding-site conformation and promotes proton exchange with the surrounding solution. Rotation thus occurs as c-subunits stochastically alternate between these environments, directionally biased by the electrochemical transmembrane gradient.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.