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

• Published in: Journal of experimental botany Vol. 53; no. 372; pp. 1321 - 1329
• Main Authors: Dietz, K.J., Horling, F., König, J., Baier, M.
• Format: Journal Article Conference Proceeding
• Language: English
• Published: Oxford Oxford University Press 01.05.2002; OXFORD UNIVERSITY PRESS; Oxford Publishing Limited (England)
• Subjects: Antioxidants; Antioxidants - metabolism; Arabidopsis; Arabidopsis - genetics; Arabidopsis - metabolism; Arabidopsis - microbiology; ascorbic acid; Ascorbic Acid - metabolism; Barley; Biochemistry; Biological and medical sciences; Catalysis; Cell biochemistry; Cell physiology; chloroplast peroxiredoxin; Chloroplasts; Chloroplasts - metabolism; Cyanobacteria - genetics; Cyanobacteria - metabolism; dehydroascorbate; DHAP; Enzymes; ferredoxin; Fundamental and applied biological sciences. Psychology; Gene Expression Regulation, Plant; Genomes; Models, Chemical; Oxidation-Reduction; Peroxidases - genetics; Peroxidases - metabolism; peroxide detoxification; Peroxides; Peroxides - metabolism; Peroxiredoxins; photosystem I; photosystem II; Phylogeny; Plant physiology and development; Plants; PSI; PSII; Reactive oxygen species; Signal Transduction; Thioredoxin; Trx; Genetic variant; Detoxification; Synechocystis; Oxidant; Review; Antioxidant; Gene expression; Metabolism; Structure function relationship; Arabidopsis thaliana; Regulation(control); Cruciferae; Dicotyledones; Angiospermae; Cyanobacteria; Bacteria; Defense mechanism; Spermatophyta; Peroxides; Intraspecific comparison; Experimental plant; Chloroplast; Enzymatic reaction
• ISSN: 0022-0957; 1460-2431; 1460-2431
• DOI: 10.1093/jexbot/53.372.1321

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.