Peroxiredoxins: A historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling

The observation that purified yeast glutamine synthetase is rapidly inactivated in a thiol-containing buffer yet retains activity in crude extracts containing the same thiol led to our discovery of an enzyme that protects against oxidation in a thiol-containing system. This novel antioxidant enzyme was shown to reduce hydroperoxides and, more recently, peroxynitrite with the use of electrons provided by a physiological thiol like thioredoxin

Sue Goo Rhee

2005

Scholarcy highlights

  • The observation that purified yeast glutamine synthetase is rapidly inactivated in a thiol-containing buffer yet retains activity in crude extracts containing the same thiol led to our discovery of an enzyme that protects against oxidation in a thiol-containing system. This novel antioxidant enzyme was shown to reduce hydroperoxides and, more recently, peroxynitrite with the use of electrons provided by a physiological thiol like thioredoxin
  • It defined a family of proteins, present in organisms from all kingdoms, that was named peroxiredoxin
  • All Prx enzymes contain a conserved Cys residue that undergoes a cycle of peroxide-dependent oxidation and thiol-dependent reduction during catalysis
  • Mammalian cells express six isoforms of Prx, which are classified into three subgroups based on the number and position of Cys residues that participate in catalysis
  • The relative abundance of Prx enzymes in mammalian cells appears to protect cellular components by removing the low levels of peroxides produced as a result of normal cellular metabolism
  • Present address: Department of Food and Nutrition, College of Home Economics, Chonnam National University, Kwanju 500-757, Korea

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