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

doi:10.1080/10715760701635082

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

Microbiology And Immunology

Research output: Contribution to journal › Article › peer-review

18 Scopus citations

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 language	English (US)
Pages (from-to)	1212-1223
Number of pages	12
Journal	Free Radical Research
Volume	41
Issue number	11
DOIs	https://doi.org/10.1080/10715760701635082
State	Published - Nov 2007

Keywords

HO
Mitochondria
Oxygen consumption
Peroxidation
Respiratory chain
Yeast

ASJC Scopus subject areas

Biochemistry

Access to Document

10.1080/10715760701635082

Cite this

Cortés-Rojo, C., Calderó;n-Cortés, E., Clemente-Guerrero, M., Manzo-Ávalos, S., Uribe, S., Boldogh, I., & Saavedra-Molina, A. (2007). Electron transport chain of Saccharomyces cerevisiae mitochondria is inhibited by H₂O₂ at succinate-cytochrome c oxidoreductase level without lipid peroxidation involvement. Free Radical Research, 41(11), 1212-1223. https://doi.org/10.1080/10715760701635082

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

Research output: Contribution to journal › Article › peer-review

Cortés-Rojo, C, Calderó;n-Cortés, E, Clemente-Guerrero, M, Manzo-Ávalos, S, Uribe, S, Boldogh, I & Saavedra-Molina, A 2007, 'Electron transport chain of Saccharomyces cerevisiae mitochondria is inhibited by H₂O₂ at succinate-cytochrome c oxidoreductase level without lipid peroxidation involvement', Free Radical Research, vol. 41, no. 11, pp. 1212-1223. https://doi.org/10.1080/10715760701635082

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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.",

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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",

note = "Funding Information: The authors appreciate the technical assistance of Norma S{\'a}nchez-Su{\'a}rez (IFC-UNAM). This study was supported partially by grants from CONACYT (AS-M: 43705, 64277; SM-A: 64308) and CIC-UMSNH (2.16) and by the P01 AG 021830 (IB) from the NIH/NIA and P01 AI062885-01 (IB) from the NIAID.",

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AU - Manzo-Ávalos, Salvador

AU - Uribe, Salvador

AU - Boldogh, Istvan

AU - Saavedra-Molina, Alfredo

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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.

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