Abstract
SEVERAL laboratories1–6 have recently been concerned with the mechanism of the bathochromic shift of about 120 nm which results when 11-cis retinal (λmax 380 nm) combines with the protein opsin to form rhodopsin (λmax 498 nm). A red shift of up to 186 nm is involved in the formation of iodopsin from 11-cis retinal and cone opsin7,8. The active site of bovine rhodopsin consists of the 11-cis retinylidene chromophore attached to a primary amine group of the protein forming a Schiff-base linkage of the type shown in Fig. 1, Ia. On the basis of the chemical reactions of rhodopsin and its derivatives it has been suggested that an interaction between a protonated form of the chromophore (structure of the type Ib) and a lipophilic environment contributes11 to the red shift.
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HIRTENSTEIN, M., AKHTAR, M. Chromcrphore-Environment Interaction of Visual Pigments in Model System. Nature New Biology 233, 94–95 (1971). https://doi.org/10.1038/newbio233094a0
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DOI: https://doi.org/10.1038/newbio233094a0
