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Mycoredoxins  are glutaredoxin-like enzymes that use mycothiol instead of glutathione as reducing cofactor. They can be considered as the glutaredoxin surrogate within mycothiol producing organism (i.e. Actinobacteria). Since the discovery of mycothiol in 1994, the existence of mycoredoxins was speculate but only in 2009 the correct protein was experimentally identified.

Exposed cysteines in proteins are extremely sensitive to oxidative stress. During a burst of oxidative stress, the cell protect these cysteine by S-thiolation with a low molecular weight thiol like mycothiol. The resulting mycothiol-protein mixed disulfide needs to be reduce to regenerate the active protein and mycothiol. Mycoredoxins specifically reduce these mixed disulfides. A such, mycoredoxins play an important role in the oxidative stress response of mycothiol producing organisms (e.g. Mycobacterium tuberculosis).

In 2012, the structure of the mycoredoxin of Mycobacterium tuberculosis was published. Mycoredoxins have a thioredoxin structural fold similar to glutaredoxins but lack the glutathione binding groove. Instead, a potential mycothiol binding site has been identified.