Interpretation of the resonance Raman spectrum of bathorhodopsin based on visual pigment analogues.
Resonance Raman spectra of visual pigment analogues have been used to evaluate various models for the structure of the retinal chromophore in bathorhodopsin. Deuteration or removal of the 18-methyl on the beta-ionyl ring or of the 19-methyl on the polyene chain demonstrates that the three intense low wavenumber bands of bathorhodopsin at 853, 875, and 920 cm-1 are not due to exomethylene or ring modes. Rather, assignment of these lines to out-of-plane vinyl hydrogen motions on the chain best accounts for the experimental data. Our calculations show that the intensity of these vibrations can be explained by twists of 10-30 degrees about chain single bonds. The 1100-1400-cm-1 Raman fingerprint indicates that the configuration of the double bonds is trans. This suggests that the structure of the bathorhodopsin chromophore is twisted all-trans.
D000818:Animals; D002417:Cattle; D008968:Molecular Conformation; D012160:Retina / Q000032:analysis; D012168:Retinal Pigments; D012172:Retinaldehyde; D012243:Rhodopsin / Q000031:analogs & derivatives*; D013059:Spectrum Analysis, Raman
D012168:Retinal Pigments; C015017:bathorhodopsin; D012243:Rhodopsin; D012172:Retinaldehyde