Cited by 131ATP Synthase and ATPases ResearchIon Transport and Channel RegulationPhotosynthetic Processes and Mechanisms

Promiscuous archaeal ATP synthase concurrently coupled to Na + and H + translocation

Open access
Schlegel, Katharina, Leone, Vanessa, Faraldo-Gómez, José D., Müller, Volker·2012·Proceedings of the National Academy of Sciences

Abstract

ATP synthases are the primary source of ATP in all living cells. To catalyze ATP synthesis, these membrane-associated complexes use a rotary mechanism powered by the transmembrane diffusion of ions down a concentration gradient. ATP synthases are assumed to be driven either by H + or Na + , reflecting distinct structural motifs in their membrane domains, and distinct metabolisms of the host organisms. Here, we study the methanogenic archaeon Methanosarcina acetivorans using assays of ATP hydrolysis and ion transport in inverted membrane vesicles, and experimentally demonstrate that the rotary mechanism of its ATP synthase is coupled to the concurrent translocation of both H + and Na + across the membrane under physiological conditions. Using free-energy molecular simulations, we explain this unprecedented observation in terms of the ion selectivity of the binding sites in the membrane rotor, which appears to have been tuned via amino acid substitutions so that ATP synthesis in M. acetivorans can be driven by the H + and Na + gradients resulting from methanogenesis. We propose that this promiscuity is a molecular mechanism of adaptation to life at the thermodynamic limit.

Integrity signals

Registry

Crossref · 10.1073/pnas.1115796109

Cites

42 of 42 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • Any improvement in coupling requires that the ancient ATPase could use Na+ ions, similar to how the modern one can.

    “Any improvement in coupling, of course, requires that the ancient ATPase could use Na+ ions, similar to how the modern one can [204,205], perhaps because hydronium ions (H3O+) have an identical charge and similar ionic radius to Na+ (ionic radii for unhydrated H3O+ = 115 pm, and for Na+ = 117 pm).”

    From Early bioenergetic evolution (2013) · cites this paper as [204]

Cites

Flagged first, then by citations

1 of the 43 references couldn’t be matched to a known paper.

Cited by

Sorted by citations

Authors
Schlegel, K., Leone, V., Faraldo-Gómez, J. D., & Müller, V.
Affiliations
  • Goethe University Frankfurt (DE)
  • Max Planck Institute of Biophysics (DE)
  • Theoretical Molecular Biophysics Group, Max Planck Institute of Biophysics, 60438 Frankfurt am Main, Germany, and
Venue
Proceedings of the National Academy of Sciences
Published
2012-01-04
Volume
109
Issue
3
Pages
947-952
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2148772877
Cited by
131
References
43
Citations by year
2026: 12 · 2025: 7 · 2024: 7 · 2023: 8 · 2022: 5 · 2021: 6 · 2020: 7 · 2019: 12 · 2018: 12 · 2017: 6 · 2016: 7 · 2015: 10 · 2014: 6 · 2013: 14 · 2012: 12
FWCI
5.40
Type
journal article
Language
en
Open access
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • Max Planck Institute for Plasma Physics (submittedVersion)
  • Max Planck Digital Library (submittedVersion)
  • MPG.PuRe (Max Planck Society) (submittedVersion)
Funders
  • Deutsche Forschungsgemeinschaft (SFB 807)
  • Senckenberg Biodiversität und Klima Forschungszentrum
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion Transport and Channel Regulation
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Photosynthetic Processes and Mechanisms
Keywords
ATP synthase, Methanosarcina acetivorans, archaea, proton translocation, sodium translocation, ion selectivity, rotary mechanism, methanogenesis, inverted membrane vesicles, ATP hydrolysis
MeSH terms
Adenosine Triphosphatases, Adenosine Triphosphate, Biological Transport, Energy Metabolism, Hydrogen-Ion Concentration, Hydrolysis, Models, Biological, Protein Binding, Protons, Sodium, Methanosarcina, Protein Subunits, Unilamellar Liposomes

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review