Evidence map›Paper›PMID 26592861›Full record

ArticleAngewandte Chemie (International ed. in English)2016

A Self-Assembled Respiratory Chain that Catalyzes NADH Oxidation by Ubiquinone-10 Cycling between Complex I and the Alternative Oxidase.

Andrew J Y Jones, James N Blaza, Hannah R Bridges, Benjamin May, Anthony L Moore, Judy Hirst

Open access · bronzeAbstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2016. 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
1.7field-weighted citation impact, top 16% 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, 50 citations in OpenAlex.

  1. Trial
  2. Improving cell-free metabolism through direct integration of artificial respiratory chains.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Decoding the Hot-Mitochondrion Paradox.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
  4. Article
  5. Global conformations ofScience advances · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. The side chain of ubiquinone plays a critical role in NaBiochimica et biophysica acta. Bioenergetics · 2022
    Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. 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

6 authors at 2 institutions in 1 country.

Andrew J Y JonesMedical Research Council Mitochondrial Biology Unit, Wellcome Trust/MRC Building, Hills Road, Cambridge, CB2 0XY (UK).
James N BlazaMedical Research Council Mitochondrial Biology Unit, Wellcome Trust/MRC Building, Hills Road, Cambridge, CB2 0XY (UK).
Hannah R BridgesMedical Research Council Mitochondrial Biology Unit, Wellcome Trust/MRC Building, Hills Road, Cambridge, CB2 0XY (UK).
Benjamin MaySchool of Life Sciences, University of Sussex, Falmer, Brighton BN1 9QG (UK).
Anthony L MooreSchool of Life Sciences, University of Sussex, Falmer, Brighton BN1 9QG (UK).
Judy HirstMedical Research Council Mitochondrial Biology Unit, Wellcome Trust/MRC Building, Hills Road, Cambridge, CB2 0XY (UK). jh@mrc-mbu.cam.ac.uk.
MRC Mitochondrial Biology Unit · GBUniversity of Sussex · GB

Funding

Biotechnology and Biological Sciences Research Council BB/L022915/1Medical Research Council MC_U105663141Medical Research Council U105663141
6 · The paper itself

Abstract

Complex I is a crucial respiratory enzyme that conserves the energy from NADH oxidation by ubiquinone-10 (Q10) in proton transport across a membrane. Studies of its energy transduction mechanism are hindered by the extreme hydrophobicity of Q10, and they have so far relied on native membranes with many components or on hydrophilic Q10 analogues that partition into membranes and undergo side reactions. Herein, we present a self-assembled system without these limitations: proteoliposomes containing mammalian complex I, Q10, and a quinol oxidase (the alternative oxidase, AOX) to recycle Q10H2 to Q10. AOX is present in excess, so complex I is completely rate determining and the Q10 pool is kept oxidized under steady-state catalysis. The system was used to measure a fully-defined K(M) value for Q10. The strategy is suitable for any enzyme with a hydrophobic quinone/quinol substrate, and could be used to characterize hydrophobic inhibitors with potential applications as pharmaceuticals, pesticides, or fungicides.

Indexed as

Alternative OxidaseCatalysisElectron TransportElectron Transport Complex IMitochondrial ProteinsNADOxidation-ReductionOxidoreductasesPlant ProteinsUbiquinoneAlternative OxidaseElectron Transport Complex IMitochondrial ProteinsNADOxidoreductasesPlant ProteinsUbiquinoneUbiquinone Q2electron transport chainNADHoxidoreductasesproteoliposomesquinones

Identifiers

PMID26592861
PMCPMC4954055
OpenAlexW2173569329

What OpenQuestion holds

Textmetadata
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.