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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Главные авторы: 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
Формат: Artigo
Язык:Inglês
Опубликовано: American Society for Biochemistry and Molecular Biology 2008
Предметы:
Enzyme Catalysis and Regulation
Online-ссылка: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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