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Biochemical properties of poplar thioredoxin z
Author(s) -
Chibani Kamel,
Tarrago Lionel,
Schürmann Peter,
Jacquot Jean-Pierre,
Rouhier Nicolas
Publication year - 2011
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2011.03.006
Subject(s) - ferredoxin thioredoxin reductase , thioredoxin , thioredoxin reductase , methionine sulfoxide reductase , ferredoxin , biochemistry , active site , enzyme , chemistry , glutaredoxin , reductase , methionine , amino acid
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.