Retinal protein interaction
Springer Online Journal Archives 1860-2000
Abstract The photoreaction of rhodopsin regenerated with 11-cis-13-demethyl-retinal was investigated by FTIR difference spectroscopy. The measurements show that the chromophore experiences different twists in the modified bathorhodopsin as compared to normal bathorhodopsin and that the twists are relaxed in the additional intermediate batho-lumirhodopsin. Whereas the missing methyl group influences the lumimetarhodopsin-I transition, a metarhodopsin-I-metarhodopsin-II difference spectrum very similar to that of unmodified rhodopsin is observed. The significance of the steric interaction for regulating the photoreaction is discussed.
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