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Anaerobic microbes: Oxygen detoxification without superoxide dismutase
  • Francis E. Jenney, Jr., Philadelphia College of Osteopathic Medicine
  • M. F. Verhagen
  • X. Cui
  • M. W. Adams
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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.

This article was published in Science, Volume 286, Issue 5438, Pages 306-309.

The published version is available at

Copyright © 1999 AAAS.

Citation Information
Francis E. Jenney, M. F. Verhagen, X. Cui and M. W. Adams. "Anaerobic microbes: Oxygen detoxification without superoxide dismutase" Science Vol. 286 (1999) p. 306 - 309
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