Studies on vision. The nature of the retinal-opsin linkage.
1. Convenient methods for the preparation of tritiated 11-cis-retinol, 11-cis-retinal and rhodopsin are described. Irradiation of labelled rhodopsin in the presence of sodium borohydride resulted in the irreversible binding of the retinyl moiety to the active site. Degradative studies established that the retinyl moiety in this reduced derivative of rhodopsin was attached to the in-amino group of lysine. In connexion with this investigation the synthesis of a number of N-retinylidene- and N-retinyl-amino acids was achieved. Derivatives of lysine with the retinyl moiety attached either to the alpha-amino group or to the in-amino group were also synthesized and characterized. 2. It is suggested that the involvement of a charge-transfer interaction between the retinylidene chromophore and a suitable group -X or -X.H on the opsin best explains the spectroscopic properties of rhodopsin and other visual proteins.
D000596:Amino Acids / Q000032:analysis; D001665:Binding Sites; D001896:Boron Compounds; D002855:Chromatography, Thin Layer; D008027:Light; D008239:Lysine; D008722:Methods; D012168:Retinal Pigments / Q000032:analysis*; D013057:Spectrum Analysis; D014316:Tritium; D014801:Vitamin A / Q000138:chemical synthesis
D000596:Amino Acids; D001896:Boron Compounds; D012168:Retinal Pigments; D014316:Tritium; D014801:Vitamin A; D008239:Lysine