Ultrafast Protein Dynamics Prior to Retinal Photoisomerization in Microbial Rhodopsins

Rhodopsins, an important group of photoreceptor proteins, possess a retinal chromophore. It has long been believed that the photoisomerization of the chromophore is the initial event triggering its photocycle. However, we recently reported that protein structural changes around the chromophore precede photoisomerization in bacteriorhodopsin (BR). In this study, we performed deep-ultraviolet femtosecond stimulated Raman measurements for H⁺-pump rhodopsin (<i>Rx</i>R) and photosensor rhodopsin (<i>Np</i>SRII) to investigate whether these ultrafast protein dynamics are common among rhodopsins. We observed that the protein structural changes occur within 0.2 ps after photoexcitation and precede the chromophore photoisomerization, similar to the case for BR. This strongly indicates that the protein structural change precedes the photoisomerization in rhodopsins, regardless of the difference in their origins and functions. Furthermore, we found that only limited protein changes occur on the time scale of the photoisomerization, suggesting that the protein environment is already optimized for the structural change of the chromophore. These observations raise the possibility that the ultrafast protein change arranges the environment around the chromophore to facilitate the photoisomerization.