The DOI matches its Crossref record; 33 of the 33 references it cites were found in a registry or an index.
Superoxide Dismutase
Open accessAbstract
An enzyme which catalyzes the dismutation of superoxide radicals (O2·- + O2·- + 2H+ → O2 + H2O2) has been purified by a simple procedure from bovine erythrocytes. This enzyme, called superoxide dismutase, contains 2 eq of copper per mole of enzyme. The copper may be reversibly removed, and it is required for activity. Superoxide dismutase has been shown to be identical with the previously described copper-containing erythrocuprein (human) and hemocuprein (bovine). Stable solutions of the superoxide radical were generated by the electrolytic reduction of O2 in an aprotic solvent, dimethylformamide. Slow infusion of such solutions into buffered aqueous media permitted the demonstration that O2·- can reduce ferricytochrome c and tetranitromethane, and that superoxide dismutase, by competing for the superoxide radicals, can markedly inhibit these reactions. Superoxide dismutase was used to show that the oxidation of epinephrine to adrenochrome by milk xanthine oxidase is mediated by the superoxide radical. An assay of several tissues indicates that superoxide dismutase is widely distributed within mammalian organisms.
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In the citing paper
“Of high importance for the mature RBC is the copper/zinc isoform 1 of SODs (SOD1), catalyzing the dismutation of the superoxide anion (Eq. 9), which is formed in RBCs mostly by Hb autoxidation (Eq. 1), into hydrogen peroxide (122).”
From Red Blood Cell Function and Dysfunction: Redox Regulation, Nitric Oxide Metabolism, Anemia (2017) · cites this paper as [122]
In the citing paper
“Of high importance for the mature RBC is the copper/zinc isoform 1 of SODs (SOD1), catalyzing the dismutation of the superoxide anion (Eq. 9), which is formed in RBCs mostly by Hb autoxidation (Eq. 1), into hydrogen peroxide (122).”
From Red Blood Cell Function and Dysfunction: Redox Regulation, Nitric Oxide Metabolism, Anemia (2017) · cites this paper as [122]
In the citing paper
“SOD was discovered in 1967 by Irwin Fridovich (McCord and Fridovich 1969).”
From Reactive Oxygen Species, Toxicity, Oxidative Stress, and Antioxidants: Chronic Diseases and Aging (2023) · cites this paper as McCord and Fridovich 1969
In the citing paper
“First, the discovery of the first antioxidant enzymes (superoxide dismutase) came decades before the discovery that non-phagocytic cells also possess enzymes (NADPH oxidases) whose sole biological function is to produce ROS 78, 79.”
From Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes (2010) · cites this paper as [78]
Citations
Cites
The Reduction of Cytochrome c by Milk Xanthine Oxidase
McCord, J. M., & Fridovich, I. (1968) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)91929-0 · Cited by 1,196
Self-citationThe microestimation of succinate and the extinction coefficient of cytochrome c
Massey, V. (1959) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(59)90259-8 · Cited by 752
The Preparation and Properties of Deflavo Xanthine Oxidase
Komai, H., Massey, V., & Palmer, G. (1969) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)91739-4 · Cited by 258
Knowles, P. F., Gibson, J. F., Pick, F. M., & Bray, R. C. (1969) · Biochemical Journal · doi:10.1042/bj1110053 · Cited by 244
Reducion of Oxygen to Superoxide Anion in Aprotic Solvents.
Maricle, D. L., & Hodgson, W. G. (1965) · Analytical Chemistry · doi:10.1021/ac60231a027 · Cited by 241
The mechanism of aerobic oxidase reaction catalyzed by peroxidase
Yamazaki, I., & Piette, L. H. (1963) · Biochimica et Biophysica Acta · doi:10.1016/0006-3002(63)90468-2 · Cited by 232
The determination of cuprous ion in copper proteins
Felsenfeld, G. (1960) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(60)90168-5 · Cited by 190
Fridovich, I., & Handler, P. (1962) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)60393-x · Cited by 189
Self-citationFridovich, I., & Handler, P. (1961) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)63312-0 · Cited by 175
Self-citationRabani, J., Mulac, W. A., & Matheson, M. S. (1965) · The Journal of Physical Chemistry · doi:10.1021/j100885a011 · Cited by 166
Research works printed but not linked: 5
- McCord, 1969, Fed. Proc., 28, 346
- Mann, 1939, Proc. Roy. Soc. Ser. B Biol. Sci., 126, 303
- Tsuchihashi, 1923, Biochem. Z., 140, 65
- Valerino, 1969, Fed. Proc., 28, 545
- Ander, 1967, Strahlentherapie, 132, 135
Cited by
Sorted by citations
Free radicals and antioxidants in normal physiological functions and human disease
Valko, M., Leibfritz, D., Moncol, J., Cronin, M. T. D., Mazur, M., & Telser, J. (2007) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2006.07.001 · Cited by 14,269
Superoxide dismutase: Improved assays and an assay applicable to acrylamide gels
Beauchamp, C., & Fridovich, I. (1971) · Analytical Biochemistry · doi:10.1016/0003-2697(71)90370-8 · Cited by 12,892
Self-citationFree Radicals in the Physiological Control of Cell Function
Dröge, W. (2002) · Physiological Reviews · doi:10.1152/physrev.00018.2001 · Cited by 9,855
Oxidants, oxidative stress and the biology of ageing
Finkel, T., & Holbrook, N. J. (2000) · Nature · doi:10.1038/35041687 · Cited by 9,413
Free radicals, metals and antioxidants in oxidative stress-induced cancer
Valko, M., Rhodes, C. J., Moncol, J., Izakovic, M., & Mazur, M. (2006) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2005.12.009 · Cited by 6,680
Metadata
- Authors
- McCord, J. M., & Fridovich, I.
- Affiliations
- Duke Medical Center (US)
- ORCID
- McCord, Joe M.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1969-11
- Volume
- 244
- Issue
- 22
- Pages
- 6049-6055
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1940436875
- Cited by
- 12,952
- References
- 33
- Citations by year
- 2026: 178 · 2025: 283 · 2024: 268 · 2023: 288 · 2022: 305 · 2021: 334 · 2020: 310 · 2019: 298 · 2018: 282 · 2017: 306 · 2016: 352 · 2015: 330 · 2014: 374 · 2013: 358 · 2012: 392
- FWCI
- 49.09
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
- Keywords
- superoxide dismutase, superoxide, copper enzymes, enzyme purification, bovine erythrocytes, ferricytochrome c reduction, tetranitromethane, epinephrine oxidation, xanthine oxidase, superoxide radical scavenging
- MeSH terms
- Adrenochrome, Alkanes, Animals, Blood Proteins, Cattle, Centrifugation, Copper, Cytochromes, Epinephrine, Erythrocytes, Free Radicals, Hydrogen Peroxide, Oxidoreductases, Oxygen, Radiochemistry, Spectrophotometry, Xanthine Oxidase
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