The structure of the retinylidene chromophore in bathorhodopsin.
Resonance Raman data on bathorhodopsin (bovine and squid) at 95,77, and 4 degrees K support a mechanism of excitation proposed by Lewis in which both a protein conformational transition and chromophore structural alteration to a "dicisoid" configuration are required to generate the bathorhodopsin species observed in steady-state photostationary mixtures. However, these results also suggest that the molecular structure with a red-shifted chromophore absorption detected at room temperatures in 1 ps using picosecond absorption spectroscopy may not necessarily have the same chromophore conformation as the steady-state bathorhodopsin species.
D000818:Animals; D049832:Decapodiformes; D011487:Protein Conformation; D012168:Retinal Pigments / Q000031:analogs & derivatives*; D012243:Rhodopsin / Q000031:analogs & derivatives*; D013059:Spectrum Analysis, Raman
D012168:Retinal Pigments; C015017:bathorhodopsin; D012243:Rhodopsin