Evidence map›Paper›PMID 32747785›Full record

ArticleNature structural & molecular biology2020

Mitochondrial complex I structure reveals ordered water molecules for catalysis and proton translocation.

Daniel N Grba, Judy Hirst

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.

0numbers the graph read from it
0cells of the map it votes in
80citing papers in PubMed
7.2field-weighted citation impact, top 2% 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

80 citing papers in PubMed, 125 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Hydration-Controlled Proton Transport in Respiratory Complex I.Journal of the American Chemical Society · 2026
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. A fixed mutation in the respiratory complex I impairs mitochondrial bioenergetics in the endangered Apennine brown bear.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  13. Global conformations ofScience advances · 2025
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

20 more citing papers are in PubMed but not listed here.

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.

Daniel N GrbaThe Medical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge, UK.ORCID http://orcid.org/0000-0003-2915-951X
Judy HirstThe Medical Research Council Mitochondrial Biology Unit, University of Cambridge, Cambridge, UK. jh@mrc-mbu.cam.ac.uk.ORCID http://orcid.org/0000-0001-8667-6797
University of Cambridge · GB

Funding

Biotechnology and Biological Sciences Research CouncilMedical Research Council MC_U105663141Medical Research Council MC_UP_1002/1Medical Research Council MC_UU_00015/2Medical Research Council MC_UU_00015/7Medical Research Council U.1056.00.023(63141)Wellcome Trust
6 · The paper itself

Abstract

Mitochondrial complex I powers ATP synthesis by oxidative phosphorylation, exploiting the energy from ubiquinone reduction by NADH to drive protons across the energy-transducing inner membrane. Recent cryo-EM analyses of mammalian and yeast complex I have revolutionized structural and mechanistic knowledge and defined structures in different functional states. Here, we describe a 2.7-Å-resolution structure of the 42-subunit complex I from the yeast Yarrowia lipolytica containing 275 structured water molecules. We identify a proton-relay pathway for ubiquinone reduction and water molecules that connect mechanistically crucial elements and constitute proton-translocation pathways through the membrane. By comparison with known structures, we deconvolute structural changes governing the mammalian 'deactive transition' (relevant to ischemia-reperfusion injury) and their effects on the ubiquinone-binding site and a connected cavity in ND1. Our structure thus provides important insights into catalysis by this enigmatic respiratory machine.

Indexed as

Binding SitesCatalysisCrystallography, X-RayElectron Transport Complex IModels, MolecularProtein ConformationProtein DomainsProtein SubunitsProtonsUbiquinoneWaterYarrowiacoenzyme Q10Electron Transport Complex IProtein SubunitsProtonsUbiquinoneWater

Identifiers

PMID32747785
PMCPMC7612091
OpenAlexW3047248739

What OpenQuestion holds

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LicenceTDM
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.