Cited by 1,616Mitochondrial Function and PathologyCardiac Ischemia and ReperfusionRedox biology and oxidative stress

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Production of Reactive Oxygen Species by Mitochondria

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Chen, Qun, Vazquez, Edwin J., Moghaddas, Shadi, Hoppel, Charles L., Lesnefsky, Edward J.·2003·Journal of Biological Chemistry

DOI 10.1074/jbc.m304854200

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Abstract

The mitochondrial respiratory chain is a major source of reactive oxygen species (ROS) under pathological conditions including myocardial ischemia and reperfusion. Limitation of electron transport by the inhibitor rotenone immediately before ischemia decreases the production of ROS in cardiac myocytes and reduces damage to mitochondria. We asked if ROS generation by intact mitochondria during the oxidation of complex I substrates (glutamate, pyruvate/malate) occurred from complex I or III. ROS production by mitochondria of Sprague-Dawley rat hearts and corresponding submitochondrial particles was studied. ROS were measured as H2O2 using the amplex red assay. In mitochondria oxidizing complex I substrates, rotenone inhibition did not increase H2O2. Oxidation of complex I or II substrates in the presence of antimycin A markedly increased H2O2. Rotenone prevented antimycin A-induced H2O2 production in mitochondria with complex I substrates but not with complex II substrates. Catalase scavenged H2O2. In contrast to intact mitochondria, blockade of complex I with rotenone markedly increased H2O2 production from submitochondrial particles oxidizing the complex I substrate NADH. ROS are produced from complex I by the NADH dehydrogenase located in the matrix side of the inner membrane and are dissipated in mitochondria by matrix antioxidant defense. However, in submitochondrial particles devoid of antioxidant defense ROS from complex I are available for detection. In mitochondria, complex III is the principal site for ROS generation during the oxidation of complex I substrates, and rotenone protects by limiting electron flow into complex III.

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Authors: Chen, Q., Vazquez, E. J., Moghaddas, S., Hoppel, C. L., & Lesnefsky, E. J.
Affiliations: Xuzhou Medical College (CN)
Louis Stokes Cleveland VA Medical Center (US)
Corresponding author: Lesnefsky, Edward J.
ORCID: Chen, Qun
Vazquez, Edwin J.
Hoppel, Charles L.
Lesnefsky, Edward J.
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 2003-09
Volume: 278
Issue: 38
Pages: 36027-36031
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.m304854200
OpenAlex: W2026525843
Cited by: 1,616
References: 39
Citations by year: 2026: 35 · 2025: 62 · 2024: 57 · 2023: 43 · 2022: 68 · 2021: 84 · 2020: 81 · 2019: 79 · 2018: 69 · 2017: 82 · 2016: 86 · 2015: 98 · 2014: 92 · 2013: 75 · 2012: 87
FWCI: 19.19
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, 6236 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: National Institutes of Health (5k04ag000676-05)
National Institute on Aging (1P0 AG15885, 1K04 AG-00676)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiac Ischemia and Reperfusion
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Keywords: reactive oxygen species, mitochondrial respiratory chain, complex I, cytochrome bc1 complex, rotenone, antimycin A, hydrogen peroxide, myocardial ischemia-reperfusion injury, NADH dehydrogenase, submitochondrial particles, catalase, glutamate oxidation
MeSH terms: Animals, Antioxidants, Binding Sites, Catalase, Electron Transport, Electrons, Hydrogen Peroxide, Ischemia, Male, Mitochondria, Models, Biological, Myocardium, NAD, NADH Dehydrogenase, Oxygen, Phosphorylation, Rotenone, Electron Transport Complex III, Reperfusion Injury, Rats, Sprague-Dawley, Reactive Oxygen Species, Succinic Acid, Myocytes, Cardiac, Rats

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Production of Reactive Oxygen Species by Mitochondria

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