A charge transfer process in the visual pigments

A physical model that incorporates all the experimental information on the formation of the visual pigment rhodopsin is presented. The visual pigments consist of a chromophore bound to an appropriate protein. Thus rhodopsin (λ_m 505 mμ) is formed by a Schiff’s base linkage C₁₉H₂₇CH=NH⁺-opsin (λ_m 440 mμ) between 11-cis retinal (λ_m 380 mμ) and the protein opsin (λ_m 280 mμ). It is found that there exists a red shift in the spectrum of rhodopsin from the Schiff’s base. The model brings an explanation for this red shift. It is shown that such a shift may be due to a charge transfer process (R. S. Mulliken,J. Am. Chem. Soc.,74, 811–824, 1952) between an electron at the double bond of carbons C₁₁−C₁₂ and an atomic orbital of the sulphur present in cysteine. This provides an explanation of the presence of SH-groups in the protein after the absorption of light. A one-electron approximation is used and the dipole momentμ _NV ; hence, the oscillator strengthf of the transitionNV is estimated and compared with the experimentally determined extinction coefficient ∈_m by mixing 3.5×10⁻³ M of 11-cis retinal with 8.3×10⁻⁵ M of cysteine at pH ranges 6 through 8. Reasonable agreement is found. Solvent, concentration and temperature dependence are shown also.