ArticleProceedings of the National Academy of Sciences of the United States of America2015
On the principle of ion selectivity in Na+/H+-coupled membrane proteins: experimental and theoretical studies of an ATP synthase rotor.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 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
21 citing papers in PubMed, 40 citations in OpenAlex.
- Uncovering hidden phylo- and ecogenomic diversity of the widespread methanotrophic genus Methylobacter.FEMS microbiology ecology · 2026Article
- Article
- Direct observation of stepping rotation of V-ATPase reveals rigid component in coupling between VProceedings of the National Academy of Sciences of the United States of America · 2022Article
- The Mechanism of Energy Coupling in HInternational journal of molecular sciences · 2022Review
- Genomic and Functional Variation of the ChlorophyllMicroorganisms · 2022Article
- ATP Synthase KFunction (Oxford, England) · 2022Article
- The 3 × 120° rotary mechanism ofProceedings of the National Academy of Sciences of the United States of America · 2020Article
- ATP synthase: Evolution, energetics, and membrane interactions.The Journal of general physiology · 2020Review
- Structural insights into sodium transport by the oxaloacetate decarboxylase sodium pump.eLife · 2020Article
- Structure of a bacterial ATP synthase.eLife · 2019Article
- Structural Asymmetry and Kinetic Limping of Single Rotary F-ATP Synthases.Molecules (Basel, Switzerland) · 2019Review
- Assembly of Spinach Chloroplast ATP Synthase Rotor Ring Protein-Lipid Complex.Frontiers in molecular biosciences · 2019Article
- Membrane plasticity facilitates recognition of the inhibitor oligomycin by the mitochondrial ATP synthase rotor.Biochimica et biophysica acta. Bioenergetics · 2018Article
- Broadly conserved NaProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Genomic Insights Into the Acid Adaptation of Novel Methanotrophs Enriched From Acidic Forest Soils.Frontiers in microbiology · 2018Article
- A symporter's secrets shown.The Journal of general physiology · 2017Article
- Thermodynamic cooperativity of cosubstrate binding and cation selectivity ofThe Journal of general physiology · 2017Article
- 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
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 3 countries.
Funding
Abstract
Numerous membrane transporters and enzymes couple their mechanisms to the permeation of Na(+) or H(+), thereby harnessing the energy stored in the form of transmembrane electrochemical potential gradients to sustain their activities. The molecular and environmental factors that control and modulate the ion specificity of most of these systems are, however, poorly understood. Here, we use isothermal titration calorimetry to determine the Na(+)/H(+) selectivity of the ion-driven membrane rotor of an F-type ATP synthase. Consistent with earlier theoretical predictions, we find that this rotor is significantly H(+) selective, although not sufficiently to be functionally coupled to H(+), owing to the large excess of Na(+) in physiological settings. The functional Na(+) specificity of this ATP synthase thus results from two opposing factors, namely its inherent chemical selectivity and the relative availability of the coupling ion. Further theoretical studies of this membrane rotor, and of two others with a much stronger and a slightly weaker H(+) selectivity, indicate that, although the inherent selectivity of their ion-binding sites is largely set by the balance of polar and hydrophobic groups flanking a conserved carboxylic side chain, subtle variations in their structure and conformational dynamics, for a similar chemical makeup, can also have a significant contribution. We propose that the principle of ion selectivity outlined here may provide a rationale for the differentiation of Na(+)- and H(+)-coupled systems in other families of membrane transporters and enzymes.
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.