Affiliation:
1. Department of Biochemistry and Molecular Biology, Center for Metalloenzyme Studies, University of Georgia, Athens, GA 30602–7229, USA.
Abstract
Superoxide reductase from the hyperthermophilic anaerobe
Pyrococcus furiosus
uses electrons from reduced nicotinamide adenine dinucleotide phosphate, by way of rubredoxin and an oxidoreductase, to reduce superoxide to hydrogen peroxide, which is then reduced to water by peroxidases. Unlike superoxide dismutase, the enzyme that protects aerobes from the toxic effects of oxygen, SOR does not catalyze the production of oxygen from superoxide and therefore confers a selective advantage on anaerobes. Superoxide reductase and associated proteins are catalytically active 80°C below the optimum growth temperature (100°C) of
P. furiosus
, conditions under which the organism is likely to be exposed to oxygen.
Publisher
American Association for the Advancement of Science (AAAS)
Cited by
355 articles.
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