Evidence map›Paper›PMID 21037553›Full record

ArticleThe EMBO journal2010

Direct observation of stepped proteolipid ring rotation in E. coli F₀F₁-ATP synthase.

Robert Ishmukhametov, Tassilo Hornung, David Spetzler, Wayne D Frasch

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
5.1field-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

47 citing papers in PubMed, 93 citations in OpenAlex.

  1. Catalytic dwell oscillations complete the FCommunications chemistry · 2025
    Article
  2. Mechanism of proton-powered c-ring rotation in a mitochondrial ATP synthase.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  3. Eukaryotic yeast VFrontiers in molecular biosciences · 2024
    Article
  4. Directed proton transfer from FBiophysical reviews · 2023
    Review
  5. Changes within the central stalk of E. coli FCommunications biology · 2023
    Article
  6. 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 · 2022
    Article
  7. Determinants of Directionality and Efficiency of the ATP Synthase FThe journal of physical chemistry letters · 2022
    Article
  8. FFrontiers in microbiology · 2022
    Review
  9. pH-dependent 11° FeLife · 2021
    Article
  10. Review
  11. Article
  12. Review
  13. The regulatory subunit ε in Escherichia coli FBiochimica et biophysica acta. Bioenergetics · 2018
    Review
  14. Article
  15. Elastic coupling power stroke mechanism of the FProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  16. Nonequilibrium fluctuations of lipid membranes by the rotating motor protein FProceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  17. Article
  18. Review
  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

4 authors at 1 institution in 1 country.

Robert IshmukhametovFaculty of Biomedicine and Biotechnology, School of Life Sciences, Arizona State University, Tempe, AZ 85287, USA.
Tassilo Hornung
David Spetzler
Wayne D Frasch
Arizona State University · US

Funding

PARTICIPATION OF METALS IN THE F1-ATPASE MECHANISMR01GM050202 · NIGMS · ARIZONA STATE UNIVERSITY-TEMPE CAMPUS · PI FRASCH, WAYNE D · 1996 to 2010
$2.3M
Fo Motor Mechanisms that Power FoF1 ATP SynthesisR01GM097510 · NIGMS · ARIZONA STATE UNIVERSITY-TEMPE CAMPUS · PI FRASCH, WAYNE D · 2011 to 2014
$1.2M
NIGMS NIH HHS R01 GM050202NIGMS NIH HHS R01 GM097510NIGMS NIH HHS R01GM50202
6 · The paper itself

Abstract

Although single-molecule experiments have provided mechanistic insight for several molecular motors, these approaches have proved difficult for membrane bound molecular motors like the F₀F₁-ATP synthase, in which proton transport across a membrane is used to synthesize ATP. Resolution of smaller steps in F₀ has been particularly hampered by signal-to-noise and time resolution. Here, we show the presence of a transient dwell between F₀ subunits a and c by improving the time resolution to 10 μs at unprecedented S/N, and by using Escherichia coli F₀F₁ embedded in lipid bilayer nanodiscs. The transient dwell interaction requires 163 μs to form and 175 μs to dissociate, is independent of proton transport residues aR210 and cD61, and behaves as a leash that allows rotary motion of the c-ring to a limit of ∼36° while engaged. This leash behaviour satisfies a requirement of a Brownian ratchet mechanism for the F₀ motor where c-ring rotational diffusion is limited to 36°.

Indexed as

Amino Acid SequenceDiffusionEscherichia coliLipid BilayersMolecular Sequence DataMutationNanotubesProteolipidsProtonsProton-Translocating ATPasesSequence AlignmentLipid BilayersProteolipidsProtonsProton-Translocating ATPases

Identifiers

PMID21037553
PMCPMC3020647
OpenAlexW2054747993

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.