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Updated: Jul 22, 2026

Simultaneous Measurement of Superoxide/Hydrogen Peroxide and NADH Production by Flavin-containing Mitochondrial Dehydrogenases
Published on: February 24, 2018
Superoxide dismutases and their impact upon human health
Felicity Johnson1, Cecilia Giulivi
1Department of Molecular Biosciences, University of California, 1311 Haring Hall, One Shields Ave, Davis, CA 95616, USA.
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.
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