Electron transfer between complexes III and IV in S. cerevisiae mitochondrial membranes.

Ana Paula Lobez, Mikael Oliveberg, Peter Brzezinski

Abstract read

In one paragraph

Article in FEBS letters, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it

0cells of the map it votes in

1citing papers in PubMed

–field-weighted citation impact

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

1 citing paper in PubMed.

Acetic acid induces strain-specific metabolic adaptation ofBiotechnology reports (Amsterdam, Netherlands) · 2026
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

3 authors.

Ana Paula LobezDepartment of Biochemistry and Biophysics, The Arrhenius Laboratories for Natural Sciences, Stockholm University, Sweden.

Mikael OlivebergDepartment of Biochemistry and Biophysics, The Arrhenius Laboratories for Natural Sciences, Stockholm University, Sweden.

Peter BrzezinskiDepartment of Biochemistry and Biophysics, The Arrhenius Laboratories for Natural Sciences, Stockholm University, Sweden.ORCID https://orcid.org/0000-0003-3860-4988

Funding

Vetenskapsrådet

6 · The paper itself

Abstract

Mitochondrial oxidative phosphorylation relies on cytochrome c transferring electrons between complexes III and IV. Earlier studies using detergent-purified complex III-IV supercomplexes from S. cerevisiae showed that this transfer is limited by two-dimensional cytochrome c diffusion. This study investigates this process in membrane-embedded mitoplasts. The results show that membrane embedment shifts the rate-limiting step from cytochrome c-mediated electron transfer to the catalytic activity of the supercomplex itself. Up to a cytochrome c : supercomplex ratio of unity, turnover increases sharply regardless of ionic strength. At higher ratios, the rate levels out at 15-20 s

Indexed as

Electron Transport Complex IIIElectron Transport Complex IVMitochondrial MembranesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCytochromes cElectron TransportOsmolar ConcentrationOxidative PhosphorylationCytochromes cElectron Transport Complex IIIElectron Transport Complex IVSaccharomyces cerevisiae Proteinscytochrome bc1cytochrome c oxidaseelectrochemical gradientelectron transferenergy conversionmembrane proteinproton transferrespiratory chainrespiratory supercomplex

Identifiers

PMID42299077

DOI10.1002/1873-3468.70382

PMCPMC13456601

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.