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Abstract
Peroxiredoxins (Prxs) are abundant low-efficiency peroxidases located in distinct cell compartments including the chloroplast and mitochondrion. They are grouped into four clans based on their structural and biochemical properties. The catalytic center contains a cysteinyl residue that reduces diverse peroxides and is regenerated via intramolecular or intermolecular thiol-disulfide-reactions and finally by electron donors such as thioredoxins and glutaredoxins. Prxs show a complex regulation by endogenous and environmental stimuli at both the transcript and protein levels. In addition to their role in antioxidant defense in photosynthesis, respiration, and stress response, they may also be involved in modulating redox signaling during development and adaptation.