Abstract
In response to reactive oxygen species (ROS), glutathione plays an important role in redox signaling by forming a disulfide bond with protein cysteine residues, known as glutathionylation. We briefly review the roles of glutathione, ROS, and glutathionylation in redox regulation. We then introduce common biochemical methods for identifying glutathionylation and highlight our recent chemical method for selective detection of glutathionylation. The merits, limitations, and future applications of our approach are also discussed.
Key words
protein cysteine modification - glutathionylation - enzyme engineering - reactive oxygen species - redox signaling