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. 2009 Oct 23;5(10):e1000541. doi: 10.1371/journal.pcbi.1000541

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This is an open-access article distributed under the terms of the Creative Commons Public Domain declaration which stipulates that, once placed in the public domain, this work may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose.

This is an open-access article distributed under the terms of the Creative Commons Public Domain declaration, which stipulates that, once placed in the public domain, this work may be freely reproduced, distributed, transmitted, modified, built upon, or otherwise used by anyone for any lawful purpose.

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A The archetypal thioredoxin reaction, entailing the reduction of a disulfide bond by a thioredoxin-like protein equipped with a dithiol CxxC active site. B The reduction of a mixed disulfide bond between glutathione and a protein by a monothiol glutaredoxin (Grx). In step I, the interaction between the hydroxyl hydrogen of a serine or threonine (green *) is suggested by conserved sequence motifs. Key: B denotes a general base. (Adapted from [70].).