Abstract
Sensory rhodopsin I (SRI), the mutated derivative SRI-D76N and the complex of SRI with its transducer HtrI were overexpressed in Halobacterium salinarium and analyzed by resonance Raman spectroscopy. In the initial state SRI contains all- trans retinal bound via a protonated Schiff base as confirmed by retinal extraction which yields 95 ± 3% all- trans retinal. The photocycle intermediate absorbing maximally at 380 nm (SRI 380) contains a Schiff base linkage between the protein and 13- cis retinal. Extraction of illuminated SRI yields up to 93% 13- cis retinal. Neither the mutation D76N nor HtrI changed the vibrational pattern of the chromophore.
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