Resonance Raman multicomponent spectra of bovine rhodopsin, isorhodopsin, and bathorhodopsin are obtained at low temperature. Application of the double beam, ‘pump‐probe’ technique allows an extraction of the rhodopsin and bathorhodopsin spectra in both protonated and deuterated media. Our results show that the Schiff bases of both rhodopsin and bathorhodopsin are fully protonated and the degree of protonation is unaffected by the rhodopsin‐bathorhodopsin transformation. Further, the data support the concept or cis‐trans isomerization as occurring in this transition. The effect of these results on various models for the primary photochemical event in vision is discussed.
|Original language||English (US)|
|Number of pages||4|
|Journal||Photochemistry and Photobiology|
|Publication status||Published - Aug 1980|
ASJC Scopus subject areas
- Physical and Theoretical Chemistry