Journal
FEBS LETTERS
Volume 585, Issue 7, Pages 1077-1081Publisher
WILEY
DOI: 10.1016/j.febslet.2011.03.006
Keywords
Chloroplast; Ferredoxin-thioredoxin reductase; Methionine sulfoxide reductase; Redox potential; Thioredoxins; Thiol-peroxidases
Funding
- INRA
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Trx-z is a chloroplastic thioredoxin, exhibiting a usual WCGPC active site, but whose biochemical properties are unknown. We demonstrate here that Trx-z supports the activity of several plastidial antioxidant enzymes, such as thiol-peroxidases and methionine sulfoxide reductases, using electrons provided by ferredoxin-thioredoxin reductase. Its disulfide reductase activity requires the presence of both active site cysteines forming a catalytic disulfide bridge with a midpoint redox potential of -251 mV at pH 7. These in vitro biochemical data suggest that, besides its decisive role in the regulation of plastidial transcription, Trx-z might also be involved in stress response. (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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