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Abstract— The contributions of different factors that might be responsible for the 500 nm absorption maximum of bovine rhodopsin are evaluated in detail. These include: (1) electrostatic interactions between the chromophore and a charged amino acid on the apoprotein; (2) exciton interactions with aromatic amino acids; (3) twisting about single bonds which have considerable double bond character; (4) weak interactions between the Schiff base and a putative counter‐ion. Analysis of these mechanisms in terms of theoretical and experimental results suggests that(2–4) are all capable of contributing to the protein induced spectral shifts. However, the “external point charge” model proposed previously, i.e. mechanism (1), appears to provide the crucial interaction. In this paper, the theoretical basis for this model is discussed in detail. The model is briefly evaluated in light of the amino‐acid sequence of bovine rhodopsin and possible implications for other visual pigments are considered.
Kakitani et al. (1985) studied this question.