Light isomerizes the chromophore of bacteriorhodopsin.
The primary photochemical event in the two light-transducing pigments whose chromophore is retinal, rhodopsin or bacteriorhodopsin, is a source of controversy. It was originally proposed that the primary photoevent in the bleaching of rhodopsin is the photoisomerization of the chromophore from 11-cis to all-trans retinal. Photochemical considerations suggested that a photoisomerization is the primary event in both rhodopsin and bacteriorhodopsin. However, this description of bacteriorhodopsin's photochemistry has been questioned. To elucidate this problem, we determined the isomeric conformation of retinal for two of the photolytic intermediates of bacteriorhodopsin, using a method that enables us to extract chromophores from the photocycle intermediates L and M at low temperatures (-74 degrees C), and have determined the isomeric conformation of the extracted retinals by HPLC. Here we provide direct evidence that isomerization of the chromophore has taken place in two of the early photocycle intermediates (L and M) of bacteriorhodopsin.
D001436:Bacteriorhodopsins / Q000528:radiation effects*; D002338:Carotenoids / Q000528:radiation effects*; D006217:Halobacterium / Q000528:radiation effects; D007536:Isomerism; D008027:Light; D010777:Photochemistry; D012172:Retinaldehyde / Q000528:radiation effects*; D014801:Vitamin A / Q000031:analogs & derivatives*
D014801:Vitamin A; D002338:Carotenoids; D001436:Bacteriorhodopsins; D012172:Retinaldehyde