SUPEROXIDE REDUCTION OF A DISULFIDE - A MODEL OF INTRACELLULAR REDOX MODULATION

被引：14

作者：

PETERSON, DA

ARCHER, SL

WEIR, EK

机构：

[1] Department of Medicine, Minneapolis VA Medical Center, University of Minnesota, Minneapolis, MN 55417, One Veterans Drive

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1994年 / 200卷 / 03期

关键词：

D O I：

10.1006/bbrc.1994.1632

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. (C) 1994 Academic Press, Inc.

引用

页码：1586 / 1591

页数：6

共 29 条

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