Charge transfer characteristics in rhodopsin mimics during photoexcitation

To gain insights into the light-harvesting capabilities of the chromophores, it is essential to understand their molecular and electronic structures within their natural chemical or biological contexts. Rhodopsins display varied absorption characteristics due to the interaction between the chromophore retinal and its surrounding protein environments. In this study, we employed a quantum mechanics/molecular mechanics approach to examine a series of artificially designed rhodopsin mimics based on human cellular retinol acid binding protein 2 (hCRABP II). We elucidated the electron transfer within the all-trans protonated Schiff base upon light excitation, and our calculated absorption spectra show well consistency with the experimental result. Furthermore, the interaction mechanisms between the chromophore and the protein were investigated, and the relationship between the blueshifts and redshifts in the absorption spectra was analyzed. Our calculation demonstrates that the blueshifts and redshifts in the rhodopsin mimics correlate well with attractive (such as the hydrogen bonds or electrostatic interactions) and repulsive interactions (such as the steric effects) between the chromophore and the protein environment, respectively. These findings could provide hints for designing rhodopsin with absorption spectra at different wavelengths.