What is the ultimate fate of superoxide anion in vivo?

Françoise Auchère, Frank Rusnak

Journal: Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry 2002;7(6):664-7

PMID: 12072975

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Abstract

For three decades, oxidative stress and the role of reactive oxygen species in biology have been extensively studied. Recently, a new interest in these areas has emerged with the discovery of superoxide reductases, a family of familiar bacterial metalloenzymes whose heretofore unknown function has now been apparently revealed. In a series of experiments utilizing genetic, molecular biological, and biochemical methods, these enzymes have been shown to be physiologically competent at removing superoxide. The role of these enzymes and their biological relationship to the well-known superoxide dismutases is discussed.

Address: Section of Hematology Research and the Department of Biochemistry & Molecular Biology, Mayo Clinic & Foundation, 200 First Street S.W., Rochester, MN 55905, USA.

DOI: 10.1007/s00775-002-0362-2

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https://dx.doi.org/10.1007/s00775-002-0362-2

MeSH Terms: Bacterial Proteins, Carrier Proteins, Desulfovibrio, Iron-Binding Proteins, Kinetics, Models, Molecular, Mycobacterium tuberculosis, Oxidation-Reduction, Oxidative Stress, Oxidoreductases, Reactive Oxygen Species, Superoxide Dismutase, Superoxides, Treponema pallidum