Fiche publication
Date publication
octobre 2018
Journal
Antioxidants (Basel, Switzerland)
Auteurs
Membres identifiés du Cancéropôle Est :
Pr BOSCHI-MULLER Sandrine
Tous les auteurs :
Boschi-Muller S
Lien Pubmed
Résumé
, an obligate pathogenic bacterium in humans, has acquired different defense mechanisms to detect and fight the oxidative stress generated by the host's defense during infection. A notable example of such a mechanism is the PilB reducing system, which repairs oxidatively-damaged methionine residues. This review will focus on the catalytic mechanism of the two methionine sulfoxide reductase (MSR) domains of PilB, which represent model enzymes for catalysis of the reduction of a sulfoxide function by thiols through sulfenic acid chemistry. The mechanism of recycling of these MSR domains by various "Trx-like" disulfide oxidoreductases will also be discussed.
Mots clés
MSR, PilB, Trx, disulfide-bond formation (Dsb) D, methionine sulfoxide, periplasm
Référence
Antioxidants (Basel). 2018 Oct 1;7(10):
