Premium
Reversible oxidation of mitochondrial peroxiredoxin 3 in mouse heart subjected to ischemia and reperfusion
Author(s) -
Kumar Vikas,
Kitaeff Nailya,
Hampton Mark B.,
Cannell Mark B.,
Winterbourn Christine C.
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.02.018
Subject(s) - peroxiredoxin , ischemia , mitochondrion , reactive oxygen species , chemistry , redox , antioxidant , cytoplasm , dimer , biochemistry , microbiology and biotechnology , biology , medicine , enzyme , peroxidase , organic chemistry
Peroxiredoxins decompose peroxides through reversible oxidation of their active site cysteines. The redox state of the 2‐Cys peroxiredoxins, 1, 2 and 3, was investigated in mouse hearts undergoing ischemia and reperfusion in a Langendorff system. The peroxiredoxins were predominantly reduced in control hearts. Mitochondrial peroxiredoxin 3 underwent significant oxidation to its disulfide‐linked dimer during ischemia. Oxidation was largely reversed during reperfusion. No redox changes in cytoplasmic peroxiredoxins 1 and 2 were apparent. Peroxiredoxin 3 oxidation suggests localized mitochondrial generation of reactive oxidants during ischemia. This local antioxidant activity of peroxiredoxin 3 may have a role in maintaining cardiac function.