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Human peroxiredoxin 5 is a peroxynitrite reductase
Author(s) -
Dubuisson Marlène,
Vander Stricht Delphine,
Clippe André,
Etienne Florence,
Nauser Thomas,
Kissner Reinhard,
Koppenol Willem H,
Rees Jean-François,
Knoops Bernard
Publication year - 2004
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.2004.06.080
Subject(s) - peroxynitrite , peroxiredoxin , chemistry , thioredoxin , biochemistry , cysteine , thioredoxin reductase , peroxidase , enzyme , superoxide
Peroxiredoxins are an ubiquitous family of peroxidases widely distributed among prokaryotes and eukaryotes. Peroxiredoxin 5, which is the last discovered mammalian member, was previously shown to reduce peroxides with the use of reducing equivalents derived from thioredoxin. We report here that human peroxiredoxin 5 is also a peroxynitrite reductase. Analysis of peroxiredoxin 5 mutants, in which each of the cysteine residues was mutated, suggests that the nucleophilic attack on the O–O bond of peroxynitrite is performed by the N‐terminal peroxidatic Cys 47 . Moreover, with the use of pulse radiolysis, we show that human peroxiredoxin 5 reduces peroxynitrite with an unequalled high rate constant of (7 ± 3) × 10 7 M −1 s −1 .