Evidence map›Paper›PMID 23893417›Full record

ArticleThe Journal of biological chemistry2013

Single-molecule analysis of F0F1-ATP synthase inhibited by N,N-dicyclohexylcarbodiimide.

Masashi Toei, Hiroyuki Noji

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.0field-weighted citation impact, top 24% 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

22 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
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  3. Review
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  6. Structure of ATP synthase from an early photosynthetic bacteriumProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Article
  8. A novelBiology methods & protocols · 2025
    Article
  9. Article
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  12. Rotation of the c-Ring Promotes the Curvature Sorting of Monomeric ATP Synthases.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Article
  13. Inhibitors of ATP Synthase as New Antibacterial Candidates.Antibiotics (Basel, Switzerland) · 2023
    Review
  14. Article
  15. ATP Synthase KFunction (Oxford, England) · 2022
    Article
  16. Article
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  18. Review
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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

2 authors at 1 institution in 1 country.

Masashi ToeiFrom the Department of Applied Chemistry, School of Engineering, University of Tokyo, Tokyo 113-8656, Japan.
Hiroyuki NojiFrom the Department of Applied Chemistry, School of Engineering, University of Tokyo, Tokyo 113-8656, Japan. Electronic address: hnoji@appchem.t.u-tokyo.ac.jp.
The University of Tokyo · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

N,N-Dicyclohexylcarbodiimide (DCCD) is a classical inhibitor of the F0F1-ATP synthase (F0F1), which covalently binds to the highly conserved carboxylic acid of the proteolipid subunit (c subunit) in F0. Although it is well known that DCCD modification of the c subunit blocks proton translocation in F0 and the coupled ATP hydrolysis activity of F1, how DCCD inhibits the rotary dynamics of F0F1 remains elusive. Here, we carried out single-molecule rotation assays to characterize the DCCD inhibition of Escherichia coli F0F1. Upon the injection of DCCD, rotations irreversibly terminated with first order reaction kinetics, suggesting that the incorporation of a single DCCD moiety is sufficient to block the rotary catalysis of the F0F1. Individual molecules terminated at different angles relative to the three catalytic angles of F1, suggesting that DCCD randomly reacts with one of the 10 c subunits. DCCD-inhibited F0F1 sometimes showed transient activation; molecules abruptly rotated and stopped after one revolution at the original termination angle, suggesting that hindrance by the DCCD moiety is released due to thermal fluctuation. To explore the mechanical activation of DCCD-inhibited molecules, we perturbed inhibited molecules using magnetic tweezers. The probability of transient activation increased upon a forward forcible rotation. Interestingly, during the termination F0F1, showed multiple positional shifts, which implies that F1 stochastically changes the angular position of its rotor upon a catalytic reaction. This effect could be caused by balancing the angular positions of the F1 and the F0 rotors, which are connected via elastic elements.

Indexed as

Adenosine TriphosphateDicyclohexylcarbodiimideEscherichia coliEscherichia coli ProteinsPropionibacteriumProtein Structure, QuaternaryProtein SubunitsProton-Translocating ATPasesAdenosine TriphosphateDicyclohexylcarbodiimideEscherichia coli ProteinsProtein SubunitsProton-Translocating ATPasesATP SynthaseEnzyme InhibitorsEnzyme KineticsEnzyme MechanismsEnzyme StructureF1F0 ATPaseProton TransportSingle-molecule Biophysics

Identifiers

PMID23893417
PMCPMC3764779
OpenAlexW2065192345

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.