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

The DOI matches its Crossref record; 33 of the 33 references it cites were found in a registry or an index.

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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Crossref · 10.1016/s0021-9258(18)63504-5

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Citations

Cites

Research works printed but not linked: 5

  1. McCord, 1969, Fed. Proc., 28, 346
  2. Mann, 1939, Proc. Roy. Soc. Ser. B Biol. Sci., 126, 303
  3. Tsuchihashi, 1923, Biochem. Z., 140, 65
  4. Valerino, 1969, Fed. Proc., 28, 545
  5. Ander, 1967, Strahlentherapie, 132, 135

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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)
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
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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