The function of peroxiredoxins in plant organelle redox metabolism

In 1996, cDNA sequences referred to as plant peroxi-redoxins (Prx), i.e. a 1-Cys Prx and a 2-Cys Prx, were reported from barley. Ten years of research have advanced our understanding of plant Prx as thiol-based peroxide reductases with a broad substrate specificity, ranging from hydrogen peroxide to alkyl hydroperox-ides and peroxinitrite. Prx have several features in common. (i) They are abundant proteins that are rou-tinely detected in proteomics approaches. (ii) They interact with proteins such as glutaredoxins, thioredox-ins, and cyclophilins as reductants, but also non-dithiol-disulphide exchange proteins. By work with transgenic plants, their activity was shown to (iii) affect metabolic integrity, (iv) protect DNA from damage in vitro an