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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...
Tallennettuna:
| Päätekijät: | , , |
|---|---|
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
American Chemical
Society
2014
|
| Linkit: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4210157/ https://ncbi.nlm.nih.gov/pubmed/25314615 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/ja506667k |
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