Evidence map›Paper›PMID 32811817›Full record

ArticleNature communications2020

Key role of quinone in the mechanism of respiratory complex I.

Javier Gutiérrez-Fernández, Karol Kaszuba, Gurdeep S Minhas, Rozbeh Baradaran, Margherita Tambalo, David T Gallagher, Leonid A Sazanov

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed, 1 pooled it
6.3field-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

60 citing papers in PubMed, 1 synthesis or guideline pooled it, 118 citations in OpenAlex.

  1. Pooled it
  2. Prediction of Ocular Toxicity of Prostaglandin FMolecules (Basel, Switzerland) · 2026
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  19. Electrochemical cofactor recycling of bacterial microcompartments.Proceedings of the National Academy of Sciences of the United States of America · 2024
    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

7 authors at 4 institutions in 3 countries.

Javier Gutiérrez-Fernández *Institute of Science and Technology Austria, Am Campus 1, A-3400, Klosterneuburg, Austria.
Karol Kaszuba *Institute of Science and Technology Austria, Am Campus 1, A-3400, Klosterneuburg, Austria.
Gurdeep S MinhasMedical Research Council Mitochondrial Biology Unit, Keith Peters Building, Hills rd, Cambridge, CB2 0XY, UK.
Rozbeh BaradaranMedical Research Council Mitochondrial Biology Unit, Keith Peters Building, Hills rd, Cambridge, CB2 0XY, UK.
Margherita TambaloInstitute of Science and Technology Austria, Am Campus 1, A-3400, Klosterneuburg, Austria.
David T GallagherMedical Research Council Mitochondrial Biology Unit, Keith Peters Building, Hills rd, Cambridge, CB2 0XY, UK.
Leonid A SazanovInstitute of Science and Technology Austria, Am Campus 1, A-3400, Klosterneuburg, Austria. sazanov@ist.ac.at.ORCID http://orcid.org/0000-0002-0977-7989
Institute of Science and Technology Austria · ATHeptares Therapeutics (United Kingdom) · GBMRC Mitochondrial Biology Unit · GBStockholm University · SE

Funding

Medical Research Council
6 · The paper itself

Abstract

Complex I is the first and the largest enzyme of respiratory chains in bacteria and mitochondria. The mechanism which couples spatially separated transfer of electrons to proton translocation in complex I is not known. Here we report five crystal structures of T. thermophilus enzyme in complex with NADH or quinone-like compounds. We also determined cryo-EM structures of major and minor native states of the complex, differing in the position of the peripheral arm. Crystal structures show that binding of quinone-like compounds (but not of NADH) leads to a related global conformational change, accompanied by local re-arrangements propagating from the quinone site to the nearest proton channel. Normal mode and molecular dynamics analyses indicate that these are likely to represent the first steps in the proton translocation mechanism. Our results suggest that quinone binding and chemistry play a key role in the coupling mechanism of complex I.

Indexed as

Molecular Dynamics SimulationAllosteric RegulationBacterial ProteinsCryoelectron MicroscopyCrystallography, X-RayElectron TransportElectron Transport Complex IModels, MolecularNADNeural Networks, ComputerProtein ConformationProtonsQuinonesThermus thermophilusBacterial ProteinsElectron Transport Complex INADProtonsQuinones

Identifiers

PMID32811817
PMCPMC7434922
OpenAlexW3055734344

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.