Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria

Turrens, J F; Boveris, A

doi:10.1042/bj1910421

Cited by 1,601Mitochondrial Function and PathologyRedox biology and oxidative stressCoenzyme Q10 studies and effects

Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria

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Turrens, J F, Boveris, A·1980·Biochemical Journal

DOI 10.1042/bj1910421PMC PMC1162232

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Abstract

Submitochondrial particles from bovine heart in which NADH dehydrogenase is reduced by either addition of NADH and rotenone or by reversed electron transfer generate 0.9 +/- 0.1 nmol of O2-/min per mg of protein at pH 7.4 and at 30 degrees C. When NADH is used as substrate, rotenone, antimycin and cyanide increase O2- production. In NADH- and antimycin-supplemented submitochondrial particles, rotenone has a biphasic effect: it increases O2- production at the NADH dehydrogenase and it inhibits O2- production at the ubiquinone-cytochrome b site. The generation of O2- by the rotenone, the uncoupler carbonyl cyanide rho-trifluoromethoxyphenylhydrazone and oligomycin at concentrations similar to those required to inhibit energy-dependent succinate-NAD reductase. Cyanide did not affect O2- generation at the NADH dehydrogenase, but inhibited O2- production at the ubiquinone-cytochrome b site. Production of O2- at the NADH dehydrogenase is about 50% of the O2- generation but the ubiquinone-cytochrome b area at pH 7.4. Additivity of the two mitochondrial sites of O2- generation was observed over the pH range from 7.0 to 8.8. AN O2–dependent autocatalytic process that requires NADH, submitochondrial particles and adrenaline is described.

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O2•− is one of the most important reactive oxygen species responsible for oxidative stress in bio-organisms and is generated as a by-product of the mitochondrial respiratory chain.
“O2•− is one of the most important reactive oxygen species ROS responsible for oxidative stress in bio-organisms and is generated as a by-product of the mitochondrial respiratory chain [8].”
From Superoxide Anion Chemistry—Its Role at the Core of the Innate Immunity (2023) · cites this paper as [8]

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Authors: Turrens, J. F., & Boveris, A.
Affiliations: Universidad de Buenos Aires (AR)
Venue: Biochemical Journal
Publisher: Portland Press Ltd.
Published: 1980-11-01
Volume: 191
Issue: 2
Pages: 421-427
ISSN: 0264-6021 (ISSN-L)
DOI: 10.1042/bj1910421
PMC: PMC1162232
OpenAlex: W2271272206
Cited by: 1,601
References: 29
Citations by year: 2026: 10 · 2025: 13 · 2024: 11 · 2023: 15 · 2022: 24 · 2021: 23 · 2020: 24 · 2019: 30 · 2018: 46 · 2017: 37 · 2016: 43 · 2015: 47 · 2014: 47 · 2013: 53 · 2012: 58
FWCI: 3.12
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Biochemical Journal (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
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: superoxide, NADH dehydrogenase, bovine heart mitochondria, rotenone, antimycin, uncoupling, oligomycin, cyanide, epinephrine, superoxide production, pH dependence
MeSH terms: Animals, Antimycin A, Cattle, Cyanides, Cytochrome Reductases, Hydrogen-Ion Concentration, Mitochondria, Heart, NADH Dehydrogenase, Oxygen, Rotenone, Submitochondrial Particles, Superoxides, In Vitro Techniques

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Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria

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