Abstract
The active-site cysteine of peroxiredoxins is selectively oxidized to cysteine sulfinic acid during catalysis, which leads to inactivation of peroxidase activity. This oxidation was thought to be irreversible. However, by metabolic labeling of mammalian cells with 35S, we show that the sulfinic form of peroxiredoxin I, produced during the exposure of cells to H2O2, is rapidly reduced to the catalytically active thiol form. The mammalian cells' ability to reduce protein sulfinic acid might serve as a mechanism to repair oxidatively damaged proteins or represent a new type of cyclic modification by which the function of various proteins is regulated.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Animals
-
Catalysis
-
Cell Line
-
Cycloheximide / pharmacology
-
Cysteine / analogs & derivatives*
-
Cysteine / metabolism*
-
Dimerization
-
HeLa Cells
-
Humans
-
Hydrogen Peroxide / metabolism*
-
Methionine / metabolism
-
Mice
-
Neurotransmitter Agents
-
Oxidation-Reduction
-
Peroxidases / chemistry
-
Peroxidases / metabolism*
-
Peroxiredoxins
-
Protein Synthesis Inhibitors / pharmacology
-
Spectrometry, Mass, Electrospray Ionization
-
Sulfhydryl Compounds / metabolism
-
Sulfinic Acids / metabolism
-
Tumor Cells, Cultured
Substances
-
Neurotransmitter Agents
-
Protein Synthesis Inhibitors
-
Sulfhydryl Compounds
-
Sulfinic Acids
-
Cycloheximide
-
Methionine
-
Hydrogen Peroxide
-
Peroxidases
-
Peroxiredoxins
-
Cysteine
-
cysteine sulfinic acid