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

Yukari Fujimoto, Jun Ishihara, Shojiro Maki, Naoko Fujioka, Tao Wang, Takumi Furuta, Nathan Fishkin, Babak Borhan, Nina Berova, Koji Nakanishi

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41 Citations (Scopus)

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 languageEnglish
Pages (from-to)4198-4204
Number of pages7
JournalChemistry - A European Journal
Volume7
Issue number19
DOIs
Publication statusPublished - 2001 Oct 1
Externally publishedYes

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Keywords

  • Chirality
  • Circular dichroism
  • Conformation analysis
  • Receptors
  • Retinal
  • Rhodopsin

ASJC Scopus subject areas

  • Catalysis
  • Organic Chemistry

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