Superoxide dismutases and their impact upon human health

Felicity Johnson, Cecilia R Giulivi

Research output: Contribution to journalArticlepeer-review

305 Scopus citations

Abstract

Superoxide dismutases (SOD), a group of metal-containing enzymes, have a vital anti-oxidant role in human health, conferred by their scavenging of one of the reactive oxygen species, superoxide anion. Three types of SODs are known in humans, with the most abundant being cytosolic SOD1, identified by its Cu, Zn-containing prosthetic group. The presence of these metals and the coordination to certain amino acids are essential for function. SODs are among the first line of defense in the detoxification of products resulting from oxidative stress. Here, we describe the importance of SOD function, and the need for coordination with other ROS-scavenging enzymes in this pathway of detoxification. The impact of metal-deficient diets (copper or zinc) or incorrect metal ion incorporation (copper chaperone for SOD) onto nascent SOD, are also examined. Finally, human pathologies associated with either SOD dysfunction or decreased activity are discussed with current progress on the development of novel therapies.

Original languageEnglish (US)
Pages (from-to)340-352
Number of pages13
JournalMolecular Aspects of Medicine
Volume26
Issue number4-5 SPEC. ISS.
DOIs
StatePublished - Aug 2005

Keywords

  • Copper-deficiency
  • Reactive nitrogen species
  • Reactive oxygen species
  • Zinc-deficiency

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Molecular Medicine

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