Evidence map›Paper›PMID 34739852›Full record

ArticleCell chemical biology2022

ND3 Cys39 in complex I is exposed during mitochondrial respiration.

Nils Burger, Andrew M James, John F Mulvey, Kurt Hoogewijs, Shujing Ding, Ian M Fearnley, Marta Loureiro-López, Abigail A I Norman, Sabine Arndt, Amin Mottahedin and 4 more

Open access · hybridAbstract read
In one paragraph

Article in Cell chemical biology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
2.9field-weighted citation impact, top 8% 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

26 citing papers in PubMed, 46 citations in OpenAlex.

  1. Article
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  3. Low oxidative stress during mitochondrial recovery from anoxia in Artemia franciscana, an invertebrate extremophile.Journal of comparative physiology. B, Biochemical, systemic, and environmental physiology · 2025
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  9. Ten "Cheat Codes" for Measuring Oxidative Stress in Humans.Antioxidants (Basel, Switzerland) · 2024
    Review
  10. Article
  11. Redox regulation of UPR signalling and mitochondrial ER contact sites.Cellular and molecular life sciences : CMLS · 2024
    Review
  12. Article
  13. Review
  14. Systems-level analyses dissociate genetic regulators of reactive oxygen species and energy production.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  15. Article
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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

14 authors at 3 institutions in 2 countries.

Nils BurgerMedical Research Council-Mitochondrial Biology Unit, University of Cambridge, Cambridge CB2 0XY, UK.
Andrew M JamesMedical Research Council-Mitochondrial Biology Unit, University of Cambridge, Cambridge CB2 0XY, UK.
John F MulveyDepartment of Medicine, University of Cambridge, Addenbrooke's Hospital, Cambridge CB2 0QQ, UK.
Kurt HoogewijsMedical Research Council-Mitochondrial Biology Unit, University of Cambridge, Cambridge CB2 0XY, UK; The Wellcome Trust Centre for Mitochondrial Research, Institute for Cell and Molecular Biosciences, Newcastle University, Newcastle Upon Tyne NE2 4HH, UK; Medical Research Council-Laboratory of Molecular Biology, Cambridge CB2 0QH, UK.
Shujing DingMedical Research Council-Mitochondrial Biology Unit, University of Cambridge, Cambridge CB2 0XY, UK.
Ian M FearnleyMedical Research Council-Mitochondrial Biology Unit, University of Cambridge, Cambridge CB2 0XY, UK.
Marta Loureiro-LópezMedical Research Council-Mitochondrial Biology Unit, University of Cambridge, Cambridge CB2 0XY, UK.
Abigail A I NormanSchool of Chemistry, University of Glasgow, Glasgow G12 8QQ, UK.
Sabine ArndtMedical Research Council-Mitochondrial Biology Unit, University of Cambridge, Cambridge CB2 0XY, UK.
Amin MottahedinMedical Research Council-Mitochondrial Biology Unit, University of Cambridge, Cambridge CB2 0XY, UK; Department of Medicine, University of Cambridge, Addenbrooke's Hospital, Cambridge CB2 0QQ, UK; Department of Physiology, Institute of Neuroscience and Physiology, Sahlgrenska Academy, University of Gothenburg, 405 30 Gothenburg, Sweden.
Olga SauchankaDepartment of Medicine, University of Cambridge, Addenbrooke's Hospital, Cambridge CB2 0QQ, UK.
Richard C HartleySchool of Chemistry, University of Glasgow, Glasgow G12 8QQ, UK.
Thomas KriegDepartment of Medicine, University of Cambridge, Addenbrooke's Hospital, Cambridge CB2 0QQ, UK.
Michael P MurphyMedical Research Council-Mitochondrial Biology Unit, University of Cambridge, Cambridge CB2 0XY, UK. Electronic address: mpm@mrc-mbu.cam.ac.uk.
University of Cambridge · GBUniversity of Glasgow · GBMRC Laboratory of Molecular Biology · GB

Funding

Medical Research Council MC_U105178803Medical Research Council MC_U105663142Medical Research Council MC_UU_00015/3Medical Research Council MC_UU_00015/7Medical Research Council MR/P000320/1Wellcome Trust 110158Wellcome Trust 110158/Z/15/ZWellcome Trust 110159Wellcome Trust 202905Wellcome Trust 206171Wellcome Trust RG88195
6 · The paper itself

Abstract

Mammalian complex I can adopt catalytically active (A-) or deactive (D-) states. A defining feature of the reversible transition between these two defined states is thought to be exposure of the ND3 subunit Cys39 residue in the D-state and its occlusion in the A-state. As the catalytic A/D transition is important in health and disease, we set out to quantify it by measuring Cys39 exposure using isotopic labeling and mass spectrometry, in parallel with complex I NADH/CoQ oxidoreductase activity. To our surprise, we found significant Cys39 exposure during NADH/CoQ oxidoreductase activity. Furthermore, this activity was unaffected if Cys39 alkylation occurred during complex I-linked respiration. In contrast, alkylation of catalytically inactive complex I irreversibly blocked the reactivation of NADH/CoQ oxidoreductase activity by NADH. Thus, Cys39 of ND3 is exposed in complex I during mitochondrial respiration, with significant implications for our understanding of the A/D transition and the mechanism of complex I.

Indexed as

Electron Transport Complex INADAnimalsCatalysisMammalsMitochondriaRespirationElectron Transport Complex INADactive/deactive transitioncomplex ICys39ischemia-reperfusion (IR) injurymitochondriaNADH:ubiquinone oxidoreductaseredox regulationreverse electron transport (RET)

Identifiers

PMID34739852
PMCPMC9076552
OpenAlexW3208478928

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.