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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SOD1 catalyzes the dismutation of the superoxide anion into hydrogen peroxide.
“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]
The superoxide anion is formed in RBCs mostly by hemoglobin autoxidation.
“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]
SOD was discovered in 1967 by Irwin Fridovich.
“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
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.
“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]
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- 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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