Electron transport chain of Saccharomyces cerevisiae mitochondria is inhibited by H2O2 at succinate-cytochrome c oxidoreductase level without lipid peroxidation involvement

Christian Cortés-Rojo, Elizabeth Calderó;n-Cortés, Mónica Clemente-Guerrero, Salvador Manzo-Ávalos, Salvador Uribe, Istvan Boldogh, Alfredo Saavedra-Molina

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

The deleterious effects of H2O2 on the electron transport chain of yeast mitochondria and on mitochondrial lipid peroxidation were evaluated. Exposure to H2O2 resulted in inhibition of the oxygen consumption in the uncoupled and phosphorylating states to 69% and 65%, respectively. The effect of H2O2 on the respiratory rate was associated with an inhibition of succinate-ubiquinone and succinate-DCIP oxidoreductase activities. Inhibitory effect of H2O2 on respiratory complexes was almost completely recovered by β-mercaptoethanol treatment. H2O2 treatment resulted in full resistance to QO site inhibitor myxothiazol and thus it is suggested that the quinol oxidase site (QO) of complex III is the target for H2O2. H2O2 did not modify basal levels of lipid peroxidation in yeast mitochondria. However, H2O2 addition to rat brain and liver mitochondria induced an increase in lipid peroxidation. These results are discussed in terms of the known physiological differences between mammalian and yeast mitochondria.

Original languageEnglish
Pages (from-to)1212-1223
Number of pages12
JournalFree Radical Research
Volume41
Issue number11
DOIs
StatePublished - Nov 2007

Fingerprint

Succinate Cytochrome c Oxidoreductase
Mitochondria
Electron Transport
Yeast
Lipid Peroxidation
Saccharomyces cerevisiae
Yeasts
Lipids
Succinic Acid
Electron Transport Complex II
Mercaptoethanol
Liver Mitochondrion
Electron Transport Complex III
Respiratory Rate
Oxygen Consumption
Ubiquinone
Liver
Rats
Brain
Oxidoreductases

Keywords

  • HO
  • Mitochondria
  • Oxygen consumption
  • Peroxidation
  • Respiratory chain
  • Yeast

ASJC Scopus subject areas

  • Biochemistry

Cite this

Electron transport chain of Saccharomyces cerevisiae mitochondria is inhibited by H2O2 at succinate-cytochrome c oxidoreductase level without lipid peroxidation involvement. / Cortés-Rojo, Christian; Calderó;n-Cortés, Elizabeth; Clemente-Guerrero, Mónica; Manzo-Ávalos, Salvador; Uribe, Salvador; Boldogh, Istvan; Saavedra-Molina, Alfredo.

In: Free Radical Research, Vol. 41, No. 11, 11.2007, p. 1212-1223.

Research output: Contribution to journalArticle

Cortés-Rojo, Christian ; Calderó;n-Cortés, Elizabeth ; Clemente-Guerrero, Mónica ; Manzo-Ávalos, Salvador ; Uribe, Salvador ; Boldogh, Istvan ; Saavedra-Molina, Alfredo. / Electron transport chain of Saccharomyces cerevisiae mitochondria is inhibited by H2O2 at succinate-cytochrome c oxidoreductase level without lipid peroxidation involvement. In: Free Radical Research. 2007 ; Vol. 41, No. 11. pp. 1212-1223.
@article{6c0f0dda57d1465aaec8f4734625b77d,
title = "Electron transport chain of Saccharomyces cerevisiae mitochondria is inhibited by H2O2 at succinate-cytochrome c oxidoreductase level without lipid peroxidation involvement",
abstract = "The deleterious effects of H2O2 on the electron transport chain of yeast mitochondria and on mitochondrial lipid peroxidation were evaluated. Exposure to H2O2 resulted in inhibition of the oxygen consumption in the uncoupled and phosphorylating states to 69{\%} and 65{\%}, respectively. The effect of H2O2 on the respiratory rate was associated with an inhibition of succinate-ubiquinone and succinate-DCIP oxidoreductase activities. Inhibitory effect of H2O2 on respiratory complexes was almost completely recovered by β-mercaptoethanol treatment. H2O2 treatment resulted in full resistance to QO site inhibitor myxothiazol and thus it is suggested that the quinol oxidase site (QO) of complex III is the target for H2O2. H2O2 did not modify basal levels of lipid peroxidation in yeast mitochondria. However, H2O2 addition to rat brain and liver mitochondria induced an increase in lipid peroxidation. These results are discussed in terms of the known physiological differences between mammalian and yeast mitochondria.",
keywords = "HO, Mitochondria, Oxygen consumption, Peroxidation, Respiratory chain, Yeast",
author = "Christian Cort{\'e}s-Rojo and Elizabeth Calder{\'o};n-Cort{\'e}s and M{\'o}nica Clemente-Guerrero and Salvador Manzo-{\'A}valos and Salvador Uribe and Istvan Boldogh and Alfredo Saavedra-Molina",
year = "2007",
month = "11",
doi = "10.1080/10715760701635082",
language = "English",
volume = "41",
pages = "1212--1223",
journal = "Free Radical Research",
issn = "1071-5762",
publisher = "Informa Healthcare",
number = "11",

}

TY - JOUR

T1 - Electron transport chain of Saccharomyces cerevisiae mitochondria is inhibited by H2O2 at succinate-cytochrome c oxidoreductase level without lipid peroxidation involvement

AU - Cortés-Rojo, Christian

AU - Calderó;n-Cortés, Elizabeth

AU - Clemente-Guerrero, Mónica

AU - Manzo-Ávalos, Salvador

AU - Uribe, Salvador

AU - Boldogh, Istvan

AU - Saavedra-Molina, Alfredo

PY - 2007/11

Y1 - 2007/11

N2 - The deleterious effects of H2O2 on the electron transport chain of yeast mitochondria and on mitochondrial lipid peroxidation were evaluated. Exposure to H2O2 resulted in inhibition of the oxygen consumption in the uncoupled and phosphorylating states to 69% and 65%, respectively. The effect of H2O2 on the respiratory rate was associated with an inhibition of succinate-ubiquinone and succinate-DCIP oxidoreductase activities. Inhibitory effect of H2O2 on respiratory complexes was almost completely recovered by β-mercaptoethanol treatment. H2O2 treatment resulted in full resistance to QO site inhibitor myxothiazol and thus it is suggested that the quinol oxidase site (QO) of complex III is the target for H2O2. H2O2 did not modify basal levels of lipid peroxidation in yeast mitochondria. However, H2O2 addition to rat brain and liver mitochondria induced an increase in lipid peroxidation. These results are discussed in terms of the known physiological differences between mammalian and yeast mitochondria.

AB - The deleterious effects of H2O2 on the electron transport chain of yeast mitochondria and on mitochondrial lipid peroxidation were evaluated. Exposure to H2O2 resulted in inhibition of the oxygen consumption in the uncoupled and phosphorylating states to 69% and 65%, respectively. The effect of H2O2 on the respiratory rate was associated with an inhibition of succinate-ubiquinone and succinate-DCIP oxidoreductase activities. Inhibitory effect of H2O2 on respiratory complexes was almost completely recovered by β-mercaptoethanol treatment. H2O2 treatment resulted in full resistance to QO site inhibitor myxothiazol and thus it is suggested that the quinol oxidase site (QO) of complex III is the target for H2O2. H2O2 did not modify basal levels of lipid peroxidation in yeast mitochondria. However, H2O2 addition to rat brain and liver mitochondria induced an increase in lipid peroxidation. These results are discussed in terms of the known physiological differences between mammalian and yeast mitochondria.

KW - HO

KW - Mitochondria

KW - Oxygen consumption

KW - Peroxidation

KW - Respiratory chain

KW - Yeast

UR - http://www.scopus.com/inward/record.url?scp=36148960929&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=36148960929&partnerID=8YFLogxK

U2 - 10.1080/10715760701635082

DO - 10.1080/10715760701635082

M3 - Article

VL - 41

SP - 1212

EP - 1223

JO - Free Radical Research

JF - Free Radical Research

SN - 1071-5762

IS - 11

ER -