Journal
ANTIOXIDANTS & REDOX SIGNALING
Volume 8, Issue 5-6, Pages 763-772Publisher
MARY ANN LIEBERT, INC
DOI: 10.1089/ars.2006.8.763
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Cysteines play an important role in protein biochemistry. The unique chemical property and high reactivity of the free thiol group makes reduced cysteine a versatile component of catalytic centers and metal binding sites in many cytosolic proteins and oxidized cystine a stabilizing component in many secreted proteins. Moreover, cysteines readily react with reactive oxygen and nitrogen species to form reversible oxidative thiol modifications. As a result, these reversible thiol modifications have found a use as regulatory nano-switches in an increasing number of redox sensitive proteins. These redox-regulated proteins are able to adjust their activity quickly in response to changes in their redox environment. Over the past few years, a number of techniques have been developed that give insight into the global thiol-disulfide state of proteins in the cell. They have been successfully used to find substrates of thiol-disulfide oxidoreductases and to discover novel redox-regulated proteins. This review will provide an overview of the current techniques, focus on approaches to quantitatively describe the extent of thiol modification in vivo, and summarize their applications.
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