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皮秒级蛋白质对光活性黄色蛋白发色团异构化的响应:通过时间分辨紫外共振拉曼光谱对酪氨酸和色氨酸残基的选择性观测

Picosecond protein response to the chromophore isomerization of photoactive yellow protein: selective observation of tyrosine and tryptophan residues by time-resolved ultraviolet resonance Raman spectroscopy.

作者信息

Mizuno Misao, Hamada Norio, Tokunaga Fumio, Mizutani Yasuhisa

出版信息

J Phys Chem B. 2007 Jun 14;111(23):6293-6. doi: 10.1021/jp072939d. Epub 2007 May 25.

Abstract

Picosecond time-resolved ultraviolet resonance Raman (UVRR) spectra of photoactive yellow protein (PYP) were measured. UVRR bands attributed to the vibration of tyrosine and tryptophan residues showed a spectral change upon photoreaction. It was found that the hydrogen-bond strength between the chromophore and Y42 increases in the pG* state. The ultrafast change in the tryptophan band revealed that a photoinduced structural change of the chromophore had propagated to the W119 region, located 12 A from the chromophore, within picoseconds.

摘要

测量了光活性黄色蛋白(PYP)的皮秒时间分辨紫外共振拉曼(UVRR)光谱。归因于酪氨酸和色氨酸残基振动的UVRR谱带在光反应后显示出光谱变化。发现在pG*状态下,发色团与Y42之间的氢键强度增加。色氨酸谱带的超快变化表明,发色团的光诱导结构变化在皮秒内传播到了距发色团12埃的W119区域。

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