Cited by 123Mitochondrial Function and PathologyRedox biology and oxidative stressCoenzyme Q10 studies and effects

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Reactive Oxygen and Targeted Antioxidant Administration in Endothelial Cell Mitochondria

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O'Malley, Yunxia, Fink, Brian D., Ross, Nicolette C., Prisinzano, Thomas E., Sivitz, William I.·2006·Journal of Biological Chemistry

DOI 10.1074/jbc.m608268200

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Abstract

We used fluorescent probes and EPR to study the mechanism(s) underlying reactive oxygen species (ROS) production by endothelial cell mitochondria and the action of mitoquinol, a mitochondria-targeted antioxidant. ROS measured by fluorescence resulted from complex I superoxide released to the matrix and converted to H(2)O(2). In contrast, EPR largely detected superoxide generated at complex III and effluxed outward. ROS fluorescence by mitochondria fueled by the complex II substrate, succinate, was substantial but markedly inhibited by rotenone. Superoxide, detected by EPR, in succinate-fueled mitochondria was not inhibited by rotenone and likely derived from semiquinone formation at complex III. Mitoquinol decreased H(2)O(2) fluorescence by succinate-fueled mitochondria but had little effect on the EPR signal for superoxide. This was not associated with a detectable decrease in membrane potential. Mitoquinol markedly enhanced ROS fluorescence in mitochondria fueled by the complex I substrates, glutamate and malate. Inhibitor studies suggested that this occurred in complex I, at one or more Q binding pockets. The above effects of mitoquinol were determined in mitochondria isolated and subsequently exposed to the targeted antioxidant. However, similar effects were observed in mitochondria after antecedent exposure to mitoquinol/mitoquinone in culture, suggesting that the agent is retained after isolation of the organelles. In conclusion, ROS production in bovine aortic endothelial cell mitochondria results largely from reverse transport to complex I and through the Q cycle in complex III. Mitoquinol blocks ROS from reverse electron transport but increases superoxide production derived from forward transport. These effects likely occur at one or more Q binding sites in complex I.

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Authors: O'Malley, Y., Fink, B. D., Ross, N. C., Prisinzano, T. E., & Sivitz, W. I.
Affiliations: University of Iowa (US)
Corresponding author: Sivitz, William I.
ORCID: Fink, Brian D.
Prisinzano, Thomas E.
Sivitz, William I.
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 2006-12
Volume: 281
Issue: 52
Pages: 39766-39775
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.m608268200
OpenAlex: W1971215002
Cited by: 123
References: 50
Citations by year: 2026: 3 · 2025: 5 · 2024: 7 · 2023: 4 · 2022: 5 · 2021: 6 · 2020: 4 · 2019: 2 · 2018: 4 · 2017: 7 · 2016: 4 · 2015: 7 · 2014: 7 · 2013: 5 · 2012: 12
FWCI: 2.99
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 5043 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: National Institute of Diabetes and Digestive and Kidney Diseases (DK-25295, P30DK025295)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Coenzyme Q10 studies and effects
Keywords: reactive oxygen species, mitochondria-targeted antioxidants, superoxide, complex I, cytochrome bc1 complex, Q-cycle, reverse electron transfer, semiquinone, rotenone, succinic acid, glutamate, malate, hydrogen peroxide, mitochondrial membrane potential
MeSH terms: Animals, Antioxidants, Cattle, Cells, Cultured, Electron Spin Resonance Spectroscopy, Endothelium, Vascular, Female, Male, Membrane Potentials, Mice, Inbred C57BL, Mitochondria, Muscle, Organophosphorus Compounds, Ubiquinone, Reactive Oxygen Species, Oxidative Stress, Mitochondrial Membranes, Mice

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Reactive Oxygen and Targeted Antioxidant Administration in Endothelial Cell Mitochondria

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