Skeletal structure of the chromophore of photoactive yellow protein in the excited state investigated by ultraviolet femtosecond stimulated Raman spectroscopy
Skeletal structure of the chromophore of photoactive yellow protein in the excited state investigated by ultraviolet femtosecond stimulated Raman spectroscopy
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紫外飞秒受激拉曼光谱研究激发态光活性黄色蛋白发色团的骨架结构
DOI：
10.1021/acs.jpcb.1c02828
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发表时间：
2021
影响因子：
3.3
通讯作者：
T. Tahara
中科院分区：
文献类型：
--
作者：
H. Kuramochi;S. Takeuchi;H. Kamikubo;M. Kataoka;T. Tahara
利用紫外飞秒受激拉曼光谱研究了光敏黄蛋白（PYP）的超快结构动力学。通过在紫外区域采用拉曼泵浦和探测脉冲，在指纹区域观察到激发态发色团的共振增强、丰富的振动特征。与溶液中激发态发色团报告的显着光谱变化相反，在蛋白质中，指纹区域中观察到的所有拉曼谱带在PYP的激发态寿命期间没有显示任何明显的光谱位移或谱带形状变化。这表明PYP在激发态时发色团没有发生明显的骨架变化，反式构象在其寿命期内保持不变。基于目前获得的PYP的飞秒拉曼光谱数据，我们讨论了PYP的激发态结构动力学的一个全面的图像。
We studied ultrafast structural dynamics of photoactive yellow protein (PYP) using ultraviolet femtosecond stimulated Raman spectroscopy. By employing the Raman pump and probe pulses in the ultraviolet region, resonantly enhanced, rich vibrational features of the excited-state chromophore were observed in the fingerprint region. In contrast to the marked spectral change reported for the excited-state chromophore in solution, in the protein, all of the observed Raman bands in the fingerprint region did not show any noticeable spectral shifts nor band shape changes during the excited-state lifetime of PYP. This indicates that the significant skeletal change does not occur on the chromophore in the excited state of PYP and that thetransconformation is retained in its lifetime. Based on the femtosecond Raman data of PYP obtained so far, we discuss a comprehensive picture of the excited-state structural dynamics of PYP.