Abstract
The visual pigments of the cones perceive red, green, and blue colors. The monkey green (MG) pigment possesses a unique Cl− binding site; however, its relationship to the spectral tuning in green pigments remains elusive. Recently, FTIR spectroscopy revealed the characteristic structural modifications of the retinal binding site by Cl− binding. Herein, we report the computational structural modeling of MG pigments and quantum-chemical simulation to investigate its spectral redshift and physicochemical relevance when Cl− is present. Our protein structures reflect the previously suggested structural changes. AlphaFold2 failed to predict these structural changes. Excited-state calculations successfully reproduced the experimental red-shifted absorption energies, corroborating our protein structures. Electrostatic energy decomposition revealed that the redshift results from the His197 protonation state and conformations of Glu129, Ser202, and Ala308; however, Cl− itself contributes to the blueshift. Site-directed mutagenesis supported our analysis. These modeled structures may provide a valuable foundation for studying cone pigments.
Supplementary materials
Title
Supplementary information
Description
Supplementary information
Actions
Title
Atomic coordinates of protein structure 1
Description
Atomic coordinates of monkey green structure (chloride bound form)
Actions
Title
Atomic coordinates of protein structure 2
Description
Atomic coordinates of monkey green structure (chloride free form)
Actions