Picosecond-Resolved Fluorescence Studies of Substrate and Cofactor-Binding Domain Mutants in a Thermophilic Alcohol Dehydrogenase Uncover an Extended Network of Communication

[Image: see text] Time-resolved fluorescence dynamics are investigated in two mutants of a thermophilic alcohol dehydrogenase (ht-ADH): Y25A (at the dimer interface) and V260A (at the cofactor-binding domain). These residues, ca. 32 Å apart, are shown to exhibit opposing low-temperature effects on t...

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Detalles Bibliográficos
Autores principales: Meadows, Corey W., Tsang, Jonathan E., Klinman, Judith P.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2014
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4210157/
https://www.ncbi.nlm.nih.gov/pubmed/25314615
http://dx.doi.org/10.1021/ja506667k

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4210157/
https://www.ncbi.nlm.nih.gov/pubmed/25314615
http://dx.doi.org/10.1021/ja506667k

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