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The Light Shall Show the Way—Or: The Conformational Changes of the Retinal Chromophore in Rhodopsin upon Light Activation
Author(s) -
Gärtner Wolfgang
Publication year - 2001
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/1521-3773(20010817)40:16<2977::aid-anie2977>3.0.co;2-e
Subject(s) - rhodopsin , chromophore , photoisomerization , visual phototransduction , retinal , heterotrimeric g protein , chemistry , moiety , photochemistry , biophysics , signal transduction , stereochemistry , g protein , isomerization , biology , biochemistry , catalysis
The visual pigment rhodopsin constitutes the interface between the physical event of light absorption and the biochemical process of visual transduction within the photoreceptor cells. The signal transduction is initiated by an 11‐ cis →all‐ trans photoisomerization of the retinal chromophore of rhodopsin which causes a series of thermally driven conformational changes of the chromophore and the protein moiety. A rhodopsin conformation is generated which allows interaction with a heterotrimeric G‐protein (see picture). Two recent publications follow the chromophore motions after light absorption by cross‐linking experiments and by solid‐state NMR spectroscopy.