Molecular and Cellular Biochemistry

, Volume 234, Issue 1, pp 3–9

Cyclic oxidation and reduction of protein methionine residues is an important antioxidant mechanism

Authors

    • Laboratory of Biochemistry, National Heart, Lung, and Blood InstituteNational Institutes of Health
  • Jackob Moskovitz
    • Laboratory of Biochemistry, National Heart, Lung, and Blood InstituteNational Institutes of Health
  • Barbara S. Berlett
    • Laboratory of Biochemistry, National Heart, Lung, and Blood InstituteNational Institutes of Health
  • Rodney L. Levine
    • Laboratory of Biochemistry, National Heart, Lung, and Blood InstituteNational Institutes of Health
Article

DOI: 10.1023/A:1015916831583

Cite this article as:
Stadtman, E.R., Moskovitz, J., Berlett, B.S. et al. Mol Cell Biochem (2002) 234: 3. doi:10.1023/A:1015916831583
  • 352 Views

Abstract

Almost all forms of reactive oxygen species (ROS) oxidize methionine residues of proteins to a mixture of the R- and S-isomers of methionine sulfoxide. Because organisms contain methionine sulfoxide reductases (Msr's) that can catalyze the thioredoxin-dependent reduction of the sulfoxides back to methionine, it was proposed that the cyclic oxidation/reduction of methionine residues might serve as antioxidants to scavenge ROS, and also to facilitate the regulation of critical enzyme activities. We summarize here results of studies showing that organisms possess two different forms of Msr – namely, MsrA that catalyzes reduction of the S-isomer and MsrB that catalyzes the reduction of the R-isomer. Deletion of the msrA gene in mice leads to increased sensitivity to oxidative stress and to a decrease (40%) in the maximum lifespan. This suggests that elimination of both Msr's would have more serious consequences.

methionine sulfoxide reductaseantioxidantsoxidative stress

Copyright information

© Kluwer Academic Publishers 2002