On the bioactive conformation of the rhodopsin chromophore: Absolute senseof twist around the 6-s-cis bond

Incubation of opsin with synthetic 6-s-locked retinoids 2a and 2b only led to pigment formation from the alpha-locked 2a, the CD spectrum of which was similar to that of native rhodopsin (Rh). This establishes that the 6-s-bo nd of the chromophore in rhodopsin is cis, and that its helicity is negativ e. Earlier cross-linking studies showed that the 11 -cis to all-trans photo isomerization occurring in the batho-Rh to lumi-Rh conversion induces a fli p over of the side carrying the ring moiety. The GTP-binding assay of pigme nt Rh-(2a), incorporating retinal analogue 2a, has shown that its activity is 80% that of the native pigment. That is. the overall conformation around the 6-s bond is retained in the steps leading to G-protein activation.