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Biochemical properties of poplar thioredoxin z.

Abstract : 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 pH7. 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.
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Kamel Chibani, Lionel Tarrago, Peter Schürmann, Jean-Pierre Jacquot, Nicolas Rouhier. Biochemical properties of poplar thioredoxin z.. FEBS Letters, Wiley, 2011, 585 (7), pp.1077-1081. ⟨10.1016/j.febslet.2011.03.006⟩. ⟨hal-02644309⟩



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