Temperature-Jump Fluorescence Provides Evidence for Fully Reversible Microsecond Dynamics in a Thermophilic Alcohol Dehydrogenase
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- 作者：Corey W. Meadows ; Gurusamy Balakrishnan ; Brandon L. Kier ; Thomas G. Spiro ; Judith P. Klinman
- 刊名：Journal of the American Chemical Society
- 出版年：2015
- 出版时间：August 19, 2015
- 年：2015
- 卷：137
- 期：32
- 页码：10060-10063
- 全文大小：295K
- ISSN：1520-5126
文摘
Protein dynamics on the microsecond (渭s) time scale were investigated by temperature-jump fluorescence spectroscopy as a function of temperature in two variants of a thermophilic alcohol dehydrogenase: W87F and W87F:H43A. Both mutants exhibit a fast, temperature-independent 渭s decrease in fluorescence followed by a slower full recovery of the initial fluorescence. The results, which rule out an ionizing histidine as the origin of the fluorescence quenching, are discussed in the context of a Trp49-containing dimer interface that acts as a conduit for thermally activated structural change within the protein interior.