Evidence map›Paper›PMID 28710385›Full record

ArticleScientific reports2017

Electron-transfer chain in respiratory complex I.

Daniel R Martin, Dmitry V Matyushov

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

24 citing papers in PubMed, 51 citations in OpenAlex.

  1. Review
  2. Article
  3. Quantum biology: From mechanisms to medicine.Clinical and translational medicine · 2026
    Review
  4. Review
  5. Article
  6. Review
  7. Article
  8. Protocellular Heme and Iron-Sulfur Clusters.Accounts of chemical research · 2024
    Review
  9. Article
  10. Review
  11. Article
  12. Iron(II)-Catalyzed Aerobic Biomimetic Oxidation of N-Heterocycles.Chemistry (Weinheim an der Bergstrasse, Germany) · 2021
    Article
  13. Efficient Aerobic Oxidation of Organic Molecules by Multistep Electron Transfer.Angewandte Chemie (International ed. in English) · 2021
    Review
  14. Article
  15. Review
  16. Bioactivity of Inhaled Methane and Interactions With Other Biological Gases.Frontiers in cell and developmental biology · 2021
    Review
  17. Article
  18. Iron(II)-Catalyzed Biomimetic Aerobic Oxidation of Alcohols.Angewandte Chemie (International ed. in English) · 2020
    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

2 authors at 1 institution in 1 country.

Daniel R MartinDepartment of Physics and School of Molecular Sciences, Arizona State University, PO Box 871504, Tempe, AZ, 85287-1504, USA.
Dmitry V MatyushovDepartment of Physics and School of Molecular Sciences, Arizona State University, PO Box 871504, Tempe, AZ, 85287-1504, USA. dmitrym@asu.edu.ORCID 0000-0002-9352-764X
Arizona State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Complex I is a part of the respiration energy chain converting the redox energy into the cross-membrane proton gradient. The electron-transfer chain of iron-sulfur cofactors within the water-soluble peripheral part of the complex is responsible for the delivery of electrons to the proton pumping subunit. The protein is porous to water penetration and the hydration level of the cofactors changes when the electron is transferred along the chain. High reaction barriers and trapping of the electrons at the iron-sulfur cofactors are prevented by the combination of intense electrostatic noise produced by the protein-water interface with the high density of quantum states in the iron-sulfur clusters caused by spin interactions between paramagnetic iron atoms. The combination of these factors substantially lowers the activation barrier for electron transfer compared to the prediction of the Marcus theory, bringing the rate to the experimentally established range. The unique role of iron-sulfur clusters as electron-transfer cofactors is in merging protein-water fluctuations with quantum-state multiplicity to allow low activation barriers and robust operation. Water plays a vital role in electron transport energetics by electrowetting the cofactors in the chain upon arrival of the electron. A general property of a protein is to violate the fluctuation-dissipation relation through nonergodic sampling of its landscape. High functional efficiency of redox enzymes is a direct consequence of nonergodicity.

Indexed as

Electron TransportElectron Transport Complex IMolecular Dynamics SimulationThermodynamicsTime FactorsWaterElectron Transport Complex IWater

Identifiers

PMID28710385
PMCPMC5511282
OpenAlexW2735568116

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.