Evidence map›Paper›PMID 29712914›Full record

ArticleNature communications2018

Structural basis for energy transduction by respiratory alternative complex III.

Joana S Sousa, Filipa Calisto, Julian D Langer, Deryck J Mills, Patrícia N Refojo, Miguel Teixeira, Werner Kühlbrandt, Janet Vonck, Manuela M Pereira

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

29 citing papers in PubMed, 49 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. A cytochrome cPlant communications · 2024
    Article
  8. DsrMKJOP is the terminal reductase complex in anaerobic sulfate respiration.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  9. Article
  10. Article
  11. Frontiers in microbiology · 2023
    Article
  12. Review
  13. Forty years in cryoEM of membrane proteins.Microscopy (Oxford, England) · 2022
    Article
  14. Article
  15. Article
  16. The MonohemeMicrobiology spectrum · 2021
    Article
  17. Article
  18. Review
  19. Review
  20. Bacterial Oxidases of the CytochromeAntioxidants & redox signaling · 2021
    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

9 authors at 3 institutions in 2 countries.

Joana S SousaDepartment of Structural Biology, Max Planck Institute of Biophysics, Max-von-Laue Str. 3, 60438, Frankfurt am Main, Germany.
Filipa CalistoInstituto de Tecnologia Química e Biológica-António Xavier, Universidade Nova de Lisboa, ITQB NOVA, Av. da República EAN, 2780-157, Oeiras, Portugal.
Julian D LangerDepartment of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max-von-Laue Str. 3, 60438, Frankfurt am Main, Germany.
Deryck J MillsDepartment of Structural Biology, Max Planck Institute of Biophysics, Max-von-Laue Str. 3, 60438, Frankfurt am Main, Germany.
Patrícia N RefojoInstituto de Tecnologia Química e Biológica-António Xavier, Universidade Nova de Lisboa, ITQB NOVA, Av. da República EAN, 2780-157, Oeiras, Portugal.
Miguel TeixeiraInstituto de Tecnologia Química e Biológica-António Xavier, Universidade Nova de Lisboa, ITQB NOVA, Av. da República EAN, 2780-157, Oeiras, Portugal.ORCID http://orcid.org/0000-0003-4124-6237
Werner KühlbrandtDepartment of Structural Biology, Max Planck Institute of Biophysics, Max-von-Laue Str. 3, 60438, Frankfurt am Main, Germany.
Janet VonckDepartment of Structural Biology, Max Planck Institute of Biophysics, Max-von-Laue Str. 3, 60438, Frankfurt am Main, Germany. janet.vonck@biophys.mpg.de.ORCID http://orcid.org/0000-0001-5659-8863
Manuela M PereiraInstituto de Tecnologia Química e Biológica-António Xavier, Universidade Nova de Lisboa, ITQB NOVA, Av. da República EAN, 2780-157, Oeiras, Portugal. mpereira@itqb.unl.pt.ORCID http://orcid.org/0000-0003-2033-4553
Max Planck Institute of Biophysics · DEUniversidade Nova de Lisboa · PTUniversity of Lisbon · PT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Electron transfer in respiratory chains generates the electrochemical potential that serves as energy source for the cell. Prokaryotes can use a wide range of electron donors and acceptors and may have alternative complexes performing the same catalytic reactions as the mitochondrial complexes. This is the case for the alternative complex III (ACIII), a quinol:cytochrome c/HiPIP oxidoreductase. In order to understand the catalytic mechanism of this respiratory enzyme, we determined the structure of ACIII from Rhodothermus marinus at 3.9 Å resolution by single-particle cryo-electron microscopy. ACIII presents a so-far unique structure, for which we establish the arrangement of the cofactors (four iron-sulfur clusters and six c-type hemes) and propose the location of the quinol-binding site and the presence of two putative proton pathways in the membrane. Altogether, this structure provides insights into a mechanism for energy transduction and introduces ACIII as a redox-driven proton pump.

Indexed as

ProtonsAmino Acid SequenceBacterial ProteinsBinding SitesCryoelectron MicroscopyElectron TransportElectron Transport Complex IIIGene ExpressionHemeHydroquinonesKineticsModels, MolecularOxidation-ReductionProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandBacterial ProteinsElectron Transport Complex IIIHemeHydroquinonesProtein SubunitsProtons

Identifiers

PMID29712914
PMCPMC5928083
OpenAlexW2802645217

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.