Mapping photoisomerization dynamics on a three-state model potential energy surface in bacteriorhodopsin using femtosecond stimulated Raman spectroscopy.

ABSTRACT: The process of proton translocation in Halobacterium salinarum, triggered by light, is powered by the photoisomerization of all-trans-retinal in bacteriorhodopsin (bR). The primary events in bR involving rapid structural changes upon light absorption occur within subpicoseconds to picoseconds. While the three-state model has received extensive support in describing the primary events between the H and K states, precise characterization of each excited state in the three-state model during photoisomerization remains elusive. In this study, we investigate the ultrafast structural dynamics of all-trans-retinal in bR using femtosecond stimulated Raman spectroscopy. We report Raman modes at 1820 cm^-1 which arise from C[double bond, length as m-dash]C stretch vibr

SUBMITTER: Wang Z 

PROVIDER: S-EPMC11775652 | biostudies-literature | 2025 Feb

REPOSITORIES: biostudies-literature