TheCorynebacterium glutamicummycothiol peroxidase is a reactive oxygen species-scavenging enzyme that shows promiscuity in thiol redox control : The mycothiol peroxidase mechanisms kinetically unraveled

Pedre, Brandán;Van Molle, Inge;Villadangos, Almudena F.;Wahni, Khadija;Messens, Joris;et.al.
(2015) Molecular Microbiology — Vol. 96, n° 6, p. 1176-1191 (2015)

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  • Pedre, Brandán
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  • Van Molle, Inge
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  • Villadangos, Almudena F.
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  • Wahni, Khadija
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  • Vertommen, Didierorcid-logoUCLouvain
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  • Messens, Joris
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Abstract
Cysteine glutathione peroxidases (CysGPxs) control oxidative stress levels by reducing hydroperoxides at the expense of cysteine thiol (-SH) oxidation, and the recovery of their peroxidatic activity is generally accomplished by thioredoxin (Trx). Corynebacterium glutamicum mycothiol peroxidase (Mpx) is a member of the CysGPx family. We discovered that its recycling is controlled by both the Trx and the mycothiol (MSH) pathway. After H2 O2 reduction, a sulfenic acid (-SOH) is formed on the peroxidatic cysteine (Cys36), which then reacts with the resolving cysteine (Cys79), forming an intramolecular disulfide (S-S), which is reduced by Trx. Alternatively, the sulfenic acid reacts with MSH and forms a mixed disulfide. Mycoredoxin 1 (Mrx1) reduces the mixed disulfide, in which Mrx1 acts in combination with MSH and mycothiol disulfide reductase as a biological relevant monothiol reducing system. Remarkably, Trx can also take over the role of Mrx1 and reduce the Mpx-MSH mixed disulfide using a dithiol mechanism. Furthermore, Mpx is important for cellular survival under H2 O2 stress, and its gene expression is clearly induced upon H2 O2 challenge. These findings add a new dimension to the redox control and the functioning of CysGPxs in general.
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Pedre, B., Van Molle, I., Villadangos, A. F., Wahni, K., Vertommen, D., Turell, L., Erdogan, H., Mateos, L. M., & Messens, J. (2015). TheCorynebacterium glutamicummycothiol peroxidase is a reactive oxygen species-scavenging enzyme that shows promiscuity in thiol redox control : The mycothiol peroxidase mechanisms kinetically unraveled. Molecular Microbiology, 96(6), 1176-1191. https://doi.org/10.1111/mmi.12998 (Original work published 2015)