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Journal of Experimental Botany, Vol. 53, No. 372, pp. 1321-1329, May 15, 2002
© 2002 Oxford University Press


Original Papers

The function of the chloroplast 2-cysteine peroxiredoxin in peroxide detoxification and its regulation

K.J. Dietz1, F. Horling, J. König and M. Baier2

University of Bielefeld, Department of Plant Physiology and Biochemistry/W5, 33501 Bielefeld, Germany

The Arabidopsis genome contains nine open reading frames with homology to members of the peroxiredoxin (prx) family: one 1-Cys-prx, two 2-Cys-prx, five type II-prx, and one peroxiredoxin Q. The function of the peroxiredoxins in plant metabolism is only slowly emerging. They are assumed to reduce toxic peroxides to their corresponding alcohols with a rather broad substrate specificity. The 2-Cys peroxiredoxins (2-CP) were recently identified as members of the antioxidant defence system of chloroplasts. Knock-out mutants of Synechocystis and antisense mutants of Arabidopsis have provided insight into the function of 2-CPs in the photosynthetic antioxidant network. This review summarizes present knowledge on the enzymatic mechanism, the physiological context and the genetic regulation of the 2-CPs in plants and cyanobacteria. In addition, an extrapolation on the metabolic role of the chloroplast 2-CP is attempted based on the molecular features of 2-CPs from other organisms.

Key words: Antioxidants, Arabidopsis, chloroplast peroxiredoxin, peroxide detoxification.


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