Superoxide Reduction of a Disulfide: A Model of Intracellular Redox Modulation?

Douglas A. Peterson, Stephen L. Archer, Kenneth K. Weir

Research output: Contribution to journalArticlepeer-review

15 Scopus citations


Superoxide dismutase (SOD), which breaks down superoxide to oxygen and hydrogen peroxide, is generally considered an antioxidant enzyme. However, superoxide is a potent reducing agent and as such could affect cellular function by reducing disulfides in important proteins, such as, ionic channels and pumps. In support of this concept, we show that superoxide, generated by two different sources, is able to reduce disulfide bonds in an in vitro model. Depending on the source of superoxide this reduction is accelerated by an unsaturated fatty acid or ferric iron and is inhibited by SOD.

Original languageEnglish (US)
Pages (from-to)1586-1591
Number of pages6
JournalBiochemical and Biophysical Research Communications
Issue number3
StatePublished - May 15 1994


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