Evidence map›Paper›PMID 22733773›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2012

Comparison of the H+/ATP ratios of the H+-ATP synthases from yeast and from chloroplast.

Jan Petersen, Kathrin Förster, Paola Turina, Peter Gräber

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

41 citing papers in PubMed, 75 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. The Warburg Effect is the result of faster ATP production by glycolysis than respiration.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Modulation of the HFrontiers in molecular biosciences · 2022
    Review
  11. Article
  12. Review
  13. The role of Cytochrome bPhotosynthesis research · 2021
    Article
  14. Review
  15. Architecture of bacterial respiratory chains.Nature reviews. Microbiology · 2021
    Review
  16. Article
  17. Article
  18. HPlant physiology · 2020
    Article
  19. Kinetic coupling of the respiratory chain with ATP synthase, but not proton gradients, drives ATP production in cristae membranes.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  20. Review
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

4 authors at 3 institutions in 3 countries.

Jan PetersenDepartment of Biochemistry and Molecular Biology, Monash University, Clayton, Victoria 3800, Australia.
Kathrin Förster
Paola Turina
Peter Gräber
University of Freiburg · DEMonash University · AUUniversity of Bologna · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

F(0)F(1)-ATP synthases use the free energy derived from a transmembrane proton transport to synthesize ATP from ADP and inorganic phosphate. The number of protons translocated per ATP (H(+)/ATP ratio) is an important parameter for the mechanism of the enzyme and for energy transduction in cells. Current models of rotational catalysis predict that the H(+)/ATP ratio is identical to the stoichiometric ratio of c-subunits to β-subunits. We measured in parallel the H(+)/ATP ratios at equilibrium of purified F(0)F(1)s from yeast mitochondria (c/β = 3.3) and from spinach chloroplasts (c/β = 4.7). The isolated enzymes were reconstituted into liposomes and, after energization of the proteoliposomes with acid-base transitions, the initial rates of ATP synthesis and hydrolysis were measured as a function of ΔpH. The equilibrium ΔpH was obtained by interpolation, and from its dependency on the stoichiometric ratio, [ATP]/([ADP]·[P(i)]), finally the thermodynamic H(+)/ATP ratios were obtained: 2.9 ± 0.2 for the mitochondrial enzyme and 3.9 ± 0.3 for the chloroplast enzyme. The data show that the thermodynamic H(+)/ATP ratio depends on the stoichiometry of the c-subunit, although it is not identical to the c/β ratio.

Indexed as

Adenosine TriphosphateATP Synthetase ComplexesBuffersCalibrationCatalysisChloroplastsEnzymesHydrogen-Ion ConcentrationHydrolysisMitochondriaModels, BiologicalProton-Motive ForceProtonsReproducibility of ResultsSaccharomyces cerevisiaeSpinacia oleraceaAdenosine TriphosphateATP Synthetase ComplexesBuffersEnzymesProtons

Identifiers

PMID22733773
PMCPMC3396544
OpenAlexW2041828183

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.