期刊
ANTIOXIDANTS
卷 7, 期 10, 页码 -出版社
MDPI
DOI: 10.3390/antiox7100131
关键词
methionine sulfoxide; MSR; PilB; Trx; periplasm; disulfide-bond formation (Dsb) D
资金
- Centre National de la Recherche Scientifique
- Universite de Lorraine
- Institut Federatif de Recherche 111 Bioingenierie
- Association pour la Recherche sur le Cancer [5436]
- French Ministry of Research (ACI IMPBio SIRE)
- French Ministry of Research (ACI BCMS047)
Neisseria meningitidis, 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.
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