Cited by 655Coenzyme Q10 studies and effectsMitochondrial Function and PathologyBioactive Compounds and Antitumor Agents

Role of ubiquinone in the mitochondrial generation of hydrogen peroxide

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Boveris, A, Cadenas, E, Stoppani, A O M·1976·Biochemical Journal

Abstract

Antimycin-inhibited bovine heart submitochondrial particles generate O2- and H2O2 with succinate as electron donor. H2O2 generation involves the action of the mitochondrial superoxide dismutase, in accordance with the McCord & Fridovich [(1969) j. biol. Chem. 244, 6049-6055] reaction mechanism. Removal of ubiquinone by acetone treatment decreases the ability of mitochondrial preparations to generate O2- and H2O2, whereas supplementation of the depleted membranes with ubiquinone enhances the peroxide-generating activity in the reconstituted membranes. Addition of superoxide dismutase to ubiquinone-reconstituted membranes is essential in order to obtain maximal rates of H2O2 generation since the acetone treatment of the membranes apparently inactivates (or removes) the mitochondrial superoxide dismutase. Parallel measurements of H2O2 production, succinate dehydrogenase and succinate-cytochrome c reductase activities show that peroxide generation by ubiquinone-supplemented membranes is a monotonous function of the reducible ubiquinone content, whereas the other two measured activities reach saturation at relatively low concentrations of reducible quinone. Alkaline treatment of submitochondrial particles causes a significant decrease in succinate dehydrogenase activity and succinate-dependent H2O2 production, which contrasts with the increase of peroxide production by the same particles with NADH as electron donor. Solubilized succinate dehydrogenase generates H2O2 at a much lower rate than the parent submitochondrial particles. It is postulated that ubisemiquinone (and ubiquinol) are chiefly responsible for the succinate-dependent peroxide production by the mitochondrial inner membrane.

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  • During hypoxia, the HIF-1α subunit becomes uninhibited by PHs, so that HIF-1α accumulates and transfers to the nucleus to initiate HIF-1α-mediated transcription of more than 70 genes involved in protein stability, such as heat-shock proteins (HSPs).

    “During hypoxia, the HIF-1α subunit becomes uninhibited by PHs, so that HIF-1α accumulates and transfers to the nucleus to initiate HIF-1α-mediated transcription of more than 70 genes involved in protein stability, such as heat-shock proteins (HSPs) (40).”

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  1. Doizaki, N. M. & Zieve, L. (1963) Proc. Soc. Exp. Biol. Med. 113,91-94
  2. Oshino, N., Oshino, R. & Chance, B. (1974) in Alcohol and Aldehyde Metabolizing Systems (Thurman, R. G., Yonetani, T., Williamson, J. R. & Chance, B., eds.), pp. 231-242, Academic Press, London and New York

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Authors
Boveris, A., Cadenas, E., & Stoppani, A. O. M.
Affiliations
Universidad de Buenos Aires (AR)
Venue
Biochemical Journal
Published
1976-05-15
Volume
156
Issue
2
Pages
435-444
ISSN
0306-3283 (ISSN-L)
OpenAlex
W1492322138
Cited by
655
References
31
Citations by year
2026: 5 · 2025: 3 · 2024: 7 · 2023: 5 · 2022: 11 · 2021: 11 · 2020: 10 · 2019: 8 · 2018: 13 · 2017: 12 · 2016: 12 · 2015: 14 · 2014: 18 · 2013: 17 · 2012: 16
FWCI
3.92
Type
journal article
Language
en
Open access
Locations
  • Biochemical Journal (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Coenzyme Q10 studies and effects
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
  • Life Sciences › Pharmacology, Toxicology and Pharmaceutics › Toxicology › Bioactive Compounds and Antitumor Agents
Keywords
coenzyme Q10, hydrogen peroxide production, mitochondrial superoxide dismutase, superoxide, succinate dehydrogenase, succinate-cytochrome c reductase, ubisemiquinone, ubiquinol, submitochondrial particles, electron transport, alkali treatment
MeSH terms
Acetone, Animals, Antimycin A, Cattle, Heart, Hydrogen Peroxide, Kinetics, Mitochondria, Mitochondria, Muscle, Myocardium, Oxygen, Phospholipids, Succinate Cytochrome c Oxidoreductase, Succinate Dehydrogenase, Succinates, Superoxide Dismutase, Ubiquinone

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