Electron transfer between complexes <scp>III</scp> and <scp>IV</scp> in <i>S. cerevisiae</i> mitochondrial membranes

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 −1 , indicating that the process is no longer limited by salinity‐dependent electron transfer, but rather by the catalytic capacity of complex IV.

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Publication Details

Journal
FEBS Letters
Published
2026-06-16
DOI
https://doi.org/10.1002/1873-3468.70382
Primary Topic
Mitochondrial Function and Pathology
Type
article
Field-Weighted Citation Impact
0.00

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article

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

Mikael Oliveberg, Peter Brzezinski, Ana Paula Lobez
FEBS Letters
Mitochondrial Function and Pathology
article

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

Mikael Oliveberg, Peter Brzezinski, Ana Paula Lobez
article en

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 −1 , indicating that the process is no longer limited by salinity‐dependent electron transfer, but rather by the catalytic capacity of complex IV.

FEBS Letters
Stockholm University (SE)
Vetenskapsrådet
Openalex Percentile: Top 12%
Mitochondrial Function and Pathology
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