Multiple functions of 2-Cys peroxiredoxins, I and II, and their regulations via post-translational modifications

Sue Goo Rhee, Hyun Ae Woo

Research output: Contribution to journalReview articlepeer-review

36 Scopus citations


Peroxiredoxins (Prxs) are an unusual family of thiol-specific peroxidases that possess a binding site for H2O2 and rely on a conserved cysteine residue for rapid reaction with H2O2. Among 6 mammalian isoforms (Prx I to VI), Prx I and Prx II are mainly found in the cytosol and nucleus. Prx I and Prx II function as antioxidant enzymes and protein chaperone under oxidative distress conditions. Under oxidative eustress conditions, Prx I and Prx II regulate the levels of H2O2 at specific area of the cells as well as sense and transduce H2O2 signaling to target proteins. Prx I and Prx II are known to be covalently modified on multiple sites: Prx I is hyperoxidized on Cys52; phosphorylated on Ser32, Thr90, and Tyr194; acetylated on Lys7, Lys16, Lys27, Lys35, and Lys197; glutathionylated on Cys52, Cys83, and Cys173; and nitrosylated on Cys52 and Cys83, whereas Prx II is hyperoxidized on Cys51; phosphorylated on Thr89, Ser112, and Thr182; acetylated on Ala2 and Lys196; glutathionylated on Cys51 and Cys172; and nitrosylated on Cys51 and Cys172. In this review, we describe how these post-translational modifications affect various functions of Prx I and Prx II.

Original languageEnglish
Pages (from-to)107-115
Number of pages9
JournalFree Radical Biology and Medicine
StatePublished - 20 May 2020

Bibliographical note

Publisher Copyright:
© 2020 The Authors


  • Acetylation
  • Chaperone
  • Glutathionylation
  • Hydrogen peroxide (HO)
  • Intracellular messenger
  • Peroxidase
  • Peroxiredoxin
  • Phosphorylation
  • S-Nitrosylation
  • Thiol oxidation


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