Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin.
The Escherichia coli periplasmic protein DsbC is active both in vivo and in vitro as a protein disulfide isomerase. For DsbC to attack incorrectly formed disulfide bonds in substrate proteins, its two active-site cysteines should be in the reduced form. Here we present evidence that, in wild-type ce...
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| Publicado en: | J Bacteriol |
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| Autores principales: | , , , |
| Formato: | Artigo |
| Lenguaje: | Inglês |
| Publicado: |
American Society for Microbiology (ASM)
1997
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| Materias: | |
| Acceso en línea: | https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC179585/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/9352906/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.179.21.6602-6608.1997 |
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