The DOI matches its Crossref record; 29 of the 29 references it cites were found in a registry or an index.
Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria
Open accessAbstract
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 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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McCord, J. M., & Fridovich, I. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)63504-5 · Cited by 12,952
Misra, H. P., & Fridovich, I. (1972) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)45228-9 · Cited by 9,097
Hydroperoxide metabolism in mammalian organs.
Chance, B., Sies, H., & Boveris, A. (1979) · Physiological Reviews · doi:10.1152/physrev.1979.59.3.527 · Cited by 5,827
Self-citationBoveris, A., & Chance, B. (1973) · Biochemical Journal · doi:10.1042/bj1340707 · Cited by 2,626
Self-citationThe Respiratory Chain and Oxidative Phosphorylation
Chance, B., & Williams, G. R. (1956) · Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjects · doi:10.1002/9780470122624.ch2 · Cited by 2,084
The cellular production of hydrogen peroxide
Boveris, A., Oshino, N., & Chance, B. (1972) · Biochemical Journal · doi:10.1042/bj1280617 · Cited by 1,549
Self-citationCadenas, E., Boveris, A., Ragan, C. I., & Stoppani, A. O. M. (1977) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(77)90035-2 · Cited by 855
Self-citationOxidases and Related Redox Systems
Milazzo, G. (1975) · Bioelectrochemistry and Bioenergetics · doi:10.1016/0302-4598(75)80018-3 · Cited by 677
Role of ubiquinone in the mitochondrial generation of hydrogen peroxide
Boveris, A., Cadenas, E., & Stoppani, A. O. M. (1976) · Biochemical Journal · doi:10.1042/bj1560435 · Cited by 655
Self-citationRespiratory chain linked H2O2 production in pigeon heart mitochondria
Loschen, G., & Flohé, L. (1971) · FEBS Letters · doi:10.1016/0014-5793(71)80459-3 · Cited by 552
Massey, V., Strickland, S., Mayhew, S. G., Howell, L. G., Engel, P. C., Matthews, R. G., Schuman, M., & Sullivan, P. A. (1969) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(69)90287-3 · Cited by 426
Fridovich, I. (1974) · Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjects · doi:10.1002/9780470122860.ch2 · Cited by 420
Boveris, A., & Cadenas, E. (1975) · FEBS Letters · doi:10.1016/0014-5793(75)80928-8 · Cited by 401
Self-citationAzzi, A., Montecucco, C., & Richter, C. (1975) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(75)80188-4 · Cited by 329
A New Look at Mechanisms in Bioenergetics
(1976) · Elsevier eBooks · doi:10.1016/b978-0-12-574670-0.x5001-8 · Cited by 316
Takeshige, K., & Minakami, S. (1979) · Biochemical Journal · doi:10.1042/bj1800129 · Cited by 299
Cadenas, E., & Boveris, A. (1980) · Biochemical Journal · doi:10.1042/bj1880031 · Cited by 275
Self-citationAdriamycin stimulated superoxide formation in submitochondrial particles
THAYER, W. S. (1977) · Chemico-Biological Interactions · doi:10.1016/0009-2797(77)90050-3 · Cited by 251
Dionisi, O., Galeotti, T., Terranova, T., & Azzi, A. (1975) · Biochimica et Biophysica Acta (BBA) - Enzymology · doi:10.1016/0005-2744(75)90059-5 · Cited by 247
MECHANISM OF THE CATALYTIC OXIDATION OF ADRENALINE BY FERRITIN
Green, S., Mazur, A., & Shorr, E. (1956) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)65348-7 · Cited by 149
The sites of superoxide anion generation in higher plant mitochondria
Rich, P. R., & Bonner, W. D. (1978) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(78)90373-9 · Cited by 146
Enzyme-catalyzed Free Radical Reactions with Nicotinamide Adenine Nucleotides
Chan, P. C., & Bielski, H. J. (1974) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)42978-5 · Cited by 101
Ohnishi, T. (1975) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(75)90087-0 · Cited by 101
Isolation and characterization of a manganese-containing superoxide dismutase from rat liver
Salin, M. L., Day, E. D., & Crapo, J. D. (1978) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(78)90027-9 · Cited by 89
Thermodynamic Relationships in Mitochondrial Oxidative Phosphorylation
Wilson, D. F., Erecińska, M., & Dutton, P. L. (1974) · Annual Review of Biophysics and Bioengineering · doi:10.1146/annurev.bb.03.060174.001223 · Cited by 87
DETECTION OF OXYGEN RADICALS IN BIOLOGICAL REACTIONS
Bors, W., Sarán, M., Lengfelder, E., Michel, C., Fuchs, C., & Frenzel, C. (1978) · Photochemistry and Photobiology · doi:10.1111/j.1751-1097.1978.tb06982.x · Cited by 80
Trumpower, B. L., & Simmons, Z. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)30054-6 · Cited by 76
Ruzicka, F. J., & Crane, F. L. (1970) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(70)90133-7 · Cited by 72
A peroxide-dependent reduction of cytochrome c by NADH
Misra, H. P., & Fridovich, I. (1973) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(73)90028-5 · Cited by 25
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Turrens, J. F. (2003) · The Journal of Physiology · doi:10.1113/jphysiol.2003.049478 · Cited by 5,084
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Forbes, J. M., & Cooper, M. E. (2013) · Physiological Reviews · doi:10.1152/physrev.00045.2011 · Cited by 2,890
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Evans, J. L., Goldfine, I. D., Maddux, B. A., & Grodsky, G. M. (2002) · Endocrine Reviews · doi:10.1210/er.2001-0039 · Cited by 2,232
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Dias, V., Junn, E., & Mouradian, M. M. (2013) · Journal of Parkinson’s Disease · doi:10.3233/jpd-130230 · Cited by 1,845
Metadata
- 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)
- 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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