Site-Directed Mutagenesis of Gln103 Reveals the Influence of This Residue on the Redox Properties and Stability of MauG

[Image: see text] The diheme enzyme MauG catalyzes a six-electron oxidation that is required for the posttranslational modification of a precursor of methylamine dehydrogenase (preMADH) to complete the biosynthesis of its protein-derived cofactor, tryptophan tryptophylquinone (TTQ). Crystallographic...

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Detalles Bibliográficos
Autores principales: Shin, Sooim, Yukl, Erik T., Sehanobish, Esha, Wilmot, Carrie M., Davidson, Victor L.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2014
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3985960/
https://www.ncbi.nlm.nih.gov/pubmed/24517455
http://dx.doi.org/10.1021/bi5000349

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3985960/
https://www.ncbi.nlm.nih.gov/pubmed/24517455
http://dx.doi.org/10.1021/bi5000349

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