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Although a great deal is known biochemically about peroxiredoxins (Prxs), little is known about their real physiological function. We show here that two cytosolic yeast Prxs, cPrxI and II, which display diversity in structure and apparent molecular weights (MW), can act alternatively as peroxidases and molecular chaperones. The peroxidase function(More)
Hydrogen peroxide (H(2)O(2)) regulates the structure and function of 2-Cys peroxiredoxins (Prxs). Upon oxidation by excess H(2)O(2), Prxs become overoxidized to a sulfinic acid of its peroxidatic cysteine residue, resulting in a structural change from a small oligomer with peroxidase function to a large oligomer with chaperone function. Then, sulfiredoxin(More)
To biochemically characterize synthetic peptides to control harmful algal blooms (HABs) that cause red tides in marine water ecosystems. We present an analysis of several short synthetic peptides and their efficacy as algicidal agents. By altering the amino acid composition of the peptides we addressed the mode of algicidal action and determine the optimal(More)
2-Cys peroxiredoxins (Prxs) play important roles in the protection of chloroplast proteins from oxidative damage. Arabidopsis NADPH-dependent thioredoxin reductase isotype C (AtNTRC) was identified as efficient electron donor for chloroplastic 2-Cys Prx-A. There are three isotypes (A, B, and C) of thioredoxin reductase (TrxR) in Arabidopsis. AtNTRA contains(More)
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