Cited by 12,952Metal-Catalyzed Oxygenation MechanismsRedox biology and oxidative stressGlutathione Transferases and Polymorphisms

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Superoxide Dismutase

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McCord, Joe M., Fridovich, Irwin·1969·Journal of Biological Chemistry

DOI 10.1016/s0021-9258(18)63504-5

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Abstract

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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The Reduction of Cytochrome c by Milk Xanthine Oxidase
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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)
DOI: 10.1016/s0021-9258(18)63504-5
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: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 18641 d)
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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