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Paradoxical redox properties of DsbB and DsbA in the protein disulfide-introducing reaction cascade

Protein disulfide bond formation in the bacterial periplasm is catalyzed by the Dsb enzymes in conjunction with the respiratory quinone components. Here we characterized redox properties of the redox active sites in DsbB to gain further insights into the catalytic mechanisms of DsbA oxidation. The s...

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Bibliografische gegevens
Hoofdauteurs: Inaba, Kenji, Ito, Koreaki
Formaat: Artigo
Taal:Inglês
Gepubliceerd in: Oxford University Press 2002
Onderwerpen:
Online toegang:https://ncbi.nlm.nih.gov/pmc/articles/PMC126043/
https://ncbi.nlm.nih.gov/pubmed/12032077
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1093/emboj/21.11.2646
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