TY - JOUR
T1 - Superoxide Reduction of a Disulfide
T2 - A Model of Intracellular Redox Modulation?
AU - Peterson, Douglas A.
AU - Archer, Stephen L.
AU - Weir, Kenneth K.
PY - 1994/5/15
Y1 - 1994/5/15
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0028198990&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0028198990&partnerID=8YFLogxK
U2 - 10.1006/bbrc.1994.1632
DO - 10.1006/bbrc.1994.1632
M3 - Article
C2 - 8185613
AN - SCOPUS:0028198990
SN - 0006-291X
VL - 200
SP - 1586
EP - 1591
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 3
ER -