Mizuno Misao, Hamada Norio, Tokunaga Fumio, Mizutani Yasuhisa
J Phys Chem B. 2007 Jun 14;111(23):6293-6. doi: 10.1021/jp072939d. Epub 2007 May 25.
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.
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。