Evidence map›Paper›PMID 20847295›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

Bioenergetic cost of making an adenosine triphosphate molecule in animal mitochondria.

Ian N Watt, Martin G Montgomery, Michael J Runswick, Andrew G W Leslie, John E Walker

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 245 papers.

0numbers the graph read from it
0cells of the map it votes in
245citing papers in PubMed
16.1field-weighted citation impact, top 1% 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

245 citing papers in PubMed, 516 citations in OpenAlex.

  1. Beyond Bioenergetics: Moonlighting Functions of FMedicinal research reviews · 2026
    Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Re-Evaluating Hot Mitochondria: Too Slow to Cool.Acta physiologica (Oxford, England) · 2026
    Review
  7. Proteolytic processing of the unique FScientific reports · 2026
    Article
  8. Review
  9. Review
  10. Cannabidiol alleviates methamphetamine addictionActa pharmaceutica Sinica. B · 2025
    Article
  11. Article
  12. Mitochondrial metabolism and cancer therapeutic innovation.Signal transduction and targeted therapy · 2025
    Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. The Role of N6-Methyladenosine in Mitochondrial Dysfunction and Pathology.International journal of molecular sciences · 2025
    Review
  18. Structure of ATP synthase from an early photosynthetic bacteriumProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  19. Article
  20. Symmetry breaking and mismatch in the torsional mechanism of ATP synthesis by FTheory in biosciences = Theorie in den Biowissenschaften · 2025
    Article

185 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Ian N WattThe Medical Research Council Mitochondrial Biology Unit, Hills Road, Cambridge, CB2 0XY, UK.
Martin G Montgomery
Michael J Runswick
Andrew G W Leslie
John E Walker
Medical Research Council · GBMRC Mitochondrial Biology Unit · GB

Funding

Medical Research Council MC_U105184325Medical Research Council MC_U105663150
6 · The paper itself

Abstract

The catalytic domain of the F-ATPase in mitochondria protrudes into the matrix of the organelle, and is attached to the membrane domain by central and peripheral stalks. Energy for the synthesis of ATP from ADP and phosphate is provided by the transmembrane proton-motive-force across the inner membrane, generated by respiration. The proton-motive force is coupled mechanically to ATP synthesis by the rotation at about 100 times per second of the central stalk and an attached ring of c-subunits in the membrane domain. Each c-subunit carries a glutamate exposed around the midpoint of the membrane on the external surface of the ring. The rotation is generated by protonation and deprotonation successively of each glutamate. Each 360° rotation produces three ATP molecules, and requires the translocation of one proton per glutamate by each c-subunit in the ring. In fungi, eubacteria, and plant chloroplasts, ring sizes of c(10)-c(15) subunits have been observed, implying that these enzymes need 3.3-5 protons to make each ATP, but until now no higher eukaryote has been examined. As shown here in the structure of the bovine F(1)-c-ring complex, the c-ring has eight c-subunits. As the sequences of c-subunits are identical throughout almost all vertebrates and are highly conserved in invertebrates, their F-ATPases probably contain c(8)-rings also. Therefore, in about 50,000 vertebrate species, and probably in many or all of the two million invertebrate species, 2.7 protons are required by the F-ATPase to make each ATP molecule.

Indexed as

Energy MetabolismAdenosine DiphosphateAdenosine TriphosphateAmino Acid SequenceAnimalsCatalysisCatalytic DomainCattleMitochondriaMolecular Sequence DataProton-Translocating ATPasesAdenosine DiphosphateAdenosine TriphosphateProton-Translocating ATPases

Identifiers

PMID20847295
PMCPMC2947889
OpenAlexW2052618584

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.