Abstract
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-bond of the chromophore in rhodopsin is cis, and that its helicity is negative. Earlier cross-linking studies showed that the 11-cis to all-trans photoisomerization occurring in the batho-Rh to lumi-Rh conversion induces a flip over of the side carrying the ring moiety. The GTP-binding assay of pigment 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.
Original language | English |
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Pages (from-to) | 4198-4204 |
Number of pages | 7 |
Journal | Chemistry - A European Journal |
Volume | 7 |
Issue number | 19 |
DOIs | |
Publication status | Published - 2001 Oct 1 |
Externally published | Yes |
Keywords
- Chirality
- Circular dichroism
- Conformation analysis
- Receptors
- Retinal
- Rhodopsin
ASJC Scopus subject areas
- Catalysis
- Organic Chemistry