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Mode of action of the thioredoxin system. Trx binds to oxidized proteins by reducing one thiol group through the formation of an intermolecular disulfide bridge. Subsequently, this mixed disulfide bridge is cleaved, also attacking the second thiol group in the protein. The second thiol group is reduced and both thiols within Trx are released from a disulfide bridge, rendering Trx inactive. TrxR recycles Trx in an NADPH-dependent manner (adapted from Karlenius and Tonissen, 2010 [29]).
