Evidence map›Paper›PMID 33768254›Full record

ArticleThe Plant cell2021

A ferredoxin bridge connects the two arms of plant mitochondrial complex I.

Niklas Klusch, Jennifer Senkler, Özkan Yildiz, Werner Kühlbrandt, Hans-Peter Braun

Open access · bronzeAbstract readVideo-Audio Media
In one paragraph

Article in The Plant cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
5.0field-weighted citation impact, top 3% 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

51 citing papers in PubMed, 85 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Global conformations ofScience advances · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Using cryo-EM to understand the assembly pathway of respiratory complex I.Acta crystallographica. Section D, Structural biology · 2024
    Article
  16. Article
  17. Protein assemblies in theFrontiers in plant science · 2024
    Article
  18. Article
  19. Article
  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

5 authors at 2 institutions in 1 country.

Niklas KluschDepartment of Structural Biology, Max-Planck-Institute of Biophysics, Frankfurt 60438, Germany.ORCID 0000-0003-2459-7377
Jennifer SenklerInstitut für Pflanzengenetik, Leibniz Universität Hannover, Hannover 30419, Germany.ORCID 0000-0002-1377-3841
Özkan YildizDepartment of Structural Biology, Max-Planck-Institute of Biophysics, Frankfurt 60438, Germany.ORCID 0000-0003-3659-2805
Werner KühlbrandtDepartment of Structural Biology, Max-Planck-Institute of Biophysics, Frankfurt 60438, Germany.ORCID 0000-0002-2013-4810
Hans-Peter BraunInstitut für Pflanzengenetik, Leibniz Universität Hannover, Hannover 30419, Germany.ORCID 0000-0002-4459-9727
Max Planck Institute of Biophysics · DELeibniz University Hannover · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mitochondrial complex I is the main site for electron transfer to the respiratory chain and generates much of the proton gradient across the inner mitochondrial membrane. Complex I is composed of two arms, which form a conserved L-shape. We report the structures of the intact, 47-subunit mitochondrial complex I from Arabidopsis thaliana and the 51-subunit complex I from the green alga Polytomella sp., both at around 2.9 Å resolution. In both complexes, a heterotrimeric γ-carbonic anhydrase domain is attached to the membrane arm on the matrix side. Two states are resolved in A. thaliana complex I, with different angles between the two arms and different conformations of the ND1 (NADH dehydrogenase subunit 1) loop near the quinol binding site. The angle appears to depend on a bridge domain, which links the peripheral arm to the membrane arm and includes an unusual ferredoxin. We propose that the bridge domain participates in regulating the activity of plant complex I.

Indexed as

ArabidopsisArabidopsis ProteinsCarbonic AnhydrasesChlorophytaCryoelectron MicroscopyElectron Transport Complex IFerredoxinsMitochondrial ProteinsModels, MolecularPlant ProteinsProtein DomainsProtein SubunitsUbiquinoneArabidopsis ProteinsCarbonic AnhydrasesElectron Transport Complex IFerredoxinsMitochondrial ProteinsPlant ProteinsProtein SubunitsUbiquinone

Identifiers

PMID33768254
PMCPMC8290278
OpenAlexW3139114646

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.