Irreversible Oxidation of the Active-site Cysteine of Peroxiredoxin to Cysteine Sulfonic Acid for Enhanced Molecular Chaperone Activity

The thiol (–SH) of the active cysteine residue in peroxiredoxin (Prx) is known to be reversibly hyperoxidized to cysteine sulfinic acid (–SO(2)H), which can be reduced back to thiol by sulfiredoxin/sestrin. However, hyperoxidized Prx of an irreversible nature has not been reported yet. Using an anti...

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Hlavní autoři: Lim, Jung Chae, Choi, Hoon-In, Park, Yu Sun, Nam, Hyung Wook, Woo, Hyun Ae, Kwon, Ki-Sun, Kim, Yu Sam, Rhee, Sue Goo, Kim, Kanghwa, Chae, Ho Zoon
Médium: Artigo
Jazyk:Inglês
Vydáno: American Society for Biochemistry and Molecular Biology 2008
Témata:
Enzyme Catalysis and Regulation
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC2662001/
https://ncbi.nlm.nih.gov/pubmed/18725414
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M804087200
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