Resonance Raman spectroscopy of squid and bovine visual pigments: the primary photochemistry in visual transduction.
Resonance Raman spectra of squid rhodopsin have been obtained under a variety of temperature and illumination conditions. The data have been characterized in terms of spectral contributions from squid rhodopsin, isorhodopsin, bathorhodopsin, lumirhodopsin, mesorhodopsin, P-465, and acid metarhodopsin. The results are compared with the spectral features obtained from bovine rhodopsin, isorhodopsin, and bathorhodopsin. The data support a proposed structure for the chromophore in bathorhodopsin which is not all trans, 11-cis, or 9-cis. This structure can be generated from either rhodopsin or isorhodopsin by a similar motion (simultaneously rotating chromophore carbon atoms 10 and 11 out-of-plane). Furthermore, we detect the same distinct bathorhodopsin vibrational modes when rhodopsin is illuminated between 4 and 100 K. This demonstrates that under steady-state illumination the light-induced chromophore structural alterations occurring at 4 K are very similar to those occurring at higher temperatures. Finally, our data indicate that bathorhodopsin is generated not only by structural transitions in the chromophore but also alterations in the opsin conformation as has recently been proposed[Lewis, A. (1978) Proc. Natl. Acad. Sci. U.S.A. 75, 549].
D000818:Animals; D002417:Cattle; D049832:Decapodiformes; D010777:Photochemistry; D012168:Retinal Pigments; D012243:Rhodopsin; D012545:Schiff Bases; D013045:Species Specificity; D013059:Spectrum Analysis, Raman; D013329:Structure-Activity Relationship; D013696:Temperature; D014785:Vision, Ocular
D012168:Retinal Pigments; D012545:Schiff Bases; D012243:Rhodopsin