Evidence map›Paper›PMID 36251339›Full record

ArticleFEBS letters2023

Single protonation of the reduced quinone in respiratory complex I drives four-proton pumping.

Alexei A Stuchebrukhov, Tomoyuki Hayashi

Open access · greenAbstract read
In one paragraph

Article in FEBS letters, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.8field-weighted citation impact, top 30% 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

5 citing papers in PubMed, 11 citations in OpenAlex.

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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

2 authors at 1 institution in 1 country.

Alexei A StuchebrukhovDepartment of Chemistry, University of California, Davis, CA, USA.ORCID https://orcid.org/0000-0002-0673-1037
Tomoyuki HayashiDepartment of Chemistry, University of California, Davis, CA, USA.
University of California, Davis · US

Funding

Theoretical Study of Charge Transfer in Cytochrome C OxidaseR01GM054052 · NIGMS · UNIVERSITY OF CALIFORNIA DAVIS · PI STUCHEBRUKHOV, ALEXEI A · 2002 to 2021
$3.3M
THEORETICAL STUDY OF BIOLOGICAL ELECTRON TRANSFERR29GM054052 · NIGMS · UNIVERSITY OF CALIFORNIA DAVIS · PI STUCHEBRUKHOV, ALEXEI A · 1996 to 2000
$101k
NIGMS NIH HHS GM054052NIGMS NIH HHS R01 GM054052NIGMS NIH HHS R29 GM054052
6 · The paper itself

Abstract

Complex I is a key proton-pumping enzyme in bacterial and mitochondrial respiratory electron transport chains. Using quantum chemistry and electrostatic calculations, we have examined the pKa of the reduced quinone QH-/QH2 in the catalytic cavity of complex I. We find that pKa (QH-/QH2) is very high, above 20. This means that the energy of a single protonation reaction of the doubly reduced quinone (i.e. the reduced semiquinone QH-) is sufficient to drive four protons across the membrane with a potential of 180 mV. Based on these calculations, we propose a possible scheme of redox-linked proton pumping by complex I. The model explains how the energy of the protonation reaction can be divided equally among four pumping units of the pump, and how a single proton can drive translocation of four additional protons in multiple pumping blocks.

Indexed as

Electron Transport Complex IProtonsBenzoquinonesElectron TransportOxidation-ReductionQuinonesBenzoquinonesElectron Transport Complex IProtonsquinoneQuinonescoupled electron-proton transferMitochondriaNADH dehydrogenaseproton pumpingproton translocationrespiratory complex I

Identifiers

PMID36251339
PMCPMC9877130
OpenAlexW4306411376

What OpenQuestion holds

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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.