Picosecond-Resolved Fluorescent Probes at Functionally Distinct Tryptophans within a Thermophilic Alcohol Dehydrogenase: Relationship of Temperature-Dependent Changes in Fluorescence to Catalysis

Two single-tryptophan variants were generated in a thermophilic alcohol dehydrogenase with the goal of correlating temperature-dependent changes in local fluorescence with the previously demonstrated catalytic break at ca. 30 °C (Kohen et al., Nature 1999, 399, 496). One tryptophan variant, W87in, r...

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Veröffentlicht in:	The journal of physical chemistry. B 2014-06, Vol.118 (23), p.6049-6061
Hauptverfasser:	Meadows, Corey W, Ou, Ryan, Klinman, Judith P
Format:	Artikel
Sprache:	eng
Schlagworte:	Acrylamide - chemistry Alcohol dehydrogenase Alcohol Dehydrogenase - chemistry Alcohol Dehydrogenase - genetics Alcohol Dehydrogenase - metabolism Bacterial Proteins - chemistry Bacterial Proteins - genetics Biocatalysis Breaking Catalysis Catalytic Domain Enzyme Stability Fluid flow Fluorescence Fluorescent Dyes - chemistry Geobacillus stearothermophilus - enzymology Kinetics Mutagenesis, Site-Directed Nanostructure Phenylalanine - chemistry Quenching Spectrometry, Fluorescence Temperature Thermodynamics Tryptophan Tryptophan - chemistry Zinc - chemistry
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