Evidence map›Paper›PMID 31964824›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2020

Kinetic coupling of the respiratory chain with ATP synthase, but not proton gradients, drives ATP production in cristae membranes.

Alexandra Toth, Axel Meyrat, Stefan Stoldt, Ricardo Santiago, Dirk Wenzel, Stefan Jakobs, Christoph von Ballmoos, Martin Ott

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
4.8field-weighted citation impact, top 4% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

53 citing papers in PubMed, 94 citations in OpenAlex.

  1. Article
  2. Proton wave propagation along collagen fibers.European biophysics journal : EBJ · 2026
    Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. Article
  8. The complexities of respiratory chain biogenesis and maintenance in yeast mitochondria.Protein science : a publication of the Protein Society · 2026
    Review
  9. ATP synthase activity boosts membrane proton acceptance and lateral diffusion.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. A splendid molecular factory: De- and reconstruction of the mammalian respiratory chain.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  16. Article
  17. Article
  18. Article
  19. Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 4 institutions in 3 countries.

Alexandra TothCenter for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden.
Axel MeyratDepartment of Chemistry and Biochemistry, University of Bern, CH-3012 Bern, Switzerland.
Stefan StoldtDepartment of NanoBiophotonics, Max Planck Institute for Biophysical Chemistry, DE-37077 Göttingen, Germany.
Ricardo SantiagoCenter for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden.
Dirk WenzelLaboratory of Electron Microscopy, Max Planck Institute for Biophysical Chemistry, DE-37077 Göttingen, Germany.
Stefan JakobsDepartment of NanoBiophotonics, Max Planck Institute for Biophysical Chemistry, DE-37077 Göttingen, Germany.ORCID 0000-0002-8028-3121
Christoph von BallmoosDepartment of Chemistry and Biochemistry, University of Bern, CH-3012 Bern, Switzerland; christoph.vonballmoos@dcb.unibe.ch martin.ott@dbb.su.se.ORCID 0000-0002-4642-6088
Martin OttCenter for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm, Sweden; christoph.vonballmoos@dcb.unibe.ch martin.ott@dbb.su.se.ORCID 0000-0001-6367-3091
Stockholm University · SEMax Planck Institute for Biophysical Chemistry · DEUniversity of Bern · CHUniversitätsmedizin Göttingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mitochondria have a characteristic ultrastructure with invaginations of the inner membrane called cristae that contain the protein complexes of the oxidative phosphorylation system. How this particular morphology of the respiratory membrane impacts energy conversion is currently unknown. One proposed role of cristae formation is to facilitate the establishment of local proton gradients to fuel ATP synthesis. Here, we determined the local pH values at defined sublocations within mitochondria of respiring yeast cells by fusing a pH-sensitive GFP to proteins residing in different mitochondrial subcompartments. Only a small proton gradient was detected over the inner membrane in wild type or cristae-lacking cells. Conversely, the obtained pH values did barely permit ATP synthesis in a reconstituted system containing purified yeast F

Indexed as

ProtonsAdenosine TriphosphateElectron TransportHydrogen-Ion ConcentrationKineticsMitochondriaMitochondrial MembranesMitochondrial Proton-Translocating ATPasesOxidative PhosphorylationProteolipidsProton PumpsSaccharomyces cerevisiaeAdenosine TriphosphateMitochondrial Proton-Translocating ATPasesProteolipidsproteoliposomesProton PumpsProtonsATP synthesiscristaeenergy conversionkinetic couplingmitochondria

Identifiers

PMID31964824
PMCPMC7007565
OpenAlexW3001989577

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.