Specific isomerization of rhodopsin-bound 11-cis-retinal to all-trans-retinal under thermal denaturation

L. J. Del Valle, E. Ramon, L. Bosch, J. Manyosa, P. Garriga

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10 Citations (Scopus)


The natural ligand of the retinal photoreceptor rhodopsin, 11-cis-retinal, is isomerized to its all-trans configuration as a consequence of light absorption in the first step of the visual phototransduction process. Here we show, by means of difference spectroscopy and high-performance liquid chromatography analysis, that thermal denaturation of rhodopsin induces the same type of isomerization. This effect is likely due to thermally induced conformational rearrangements of amino acid residues in the retinal-binding pocket - possibly implying helical movements - and highlights the tight coupling between 11-cis-retinal and opsin. This effect could have implications in the instability and functional changes seen for certain mutations in rhodopsin associated with retinal disease, and in the stability of the different conformers induced by mutations in other G protein-coupled receptors.
Original languageEnglish
Pages (from-to)2532-2537
JournalCellular and Molecular Life Sciences
Issue number11
Publication statusPublished - 1 Nov 2003


  • 11-cis-retinal
  • All-trans-retinal
  • G protein-coupled receptor
  • Membrane protein
  • Retinal-binding pocket
  • Rhodopsin
  • Thermal stability


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