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Influence of Arrestin on the Photodecay of Bovine Rhodopsin
Author(s) -
Chatterjee Deep,
Eckert Carl Elias,
Slavov Chavdar,
Saxena Krishna,
Fürtig Boris,
Sanders Charles R.,
Gurevich Vsevolod V.,
Wachtveitl Josef,
Schwalbe Harald
Publication year - 2015
Publication title -
angewandte chemie
Language(s) - English
Resource type - Journals
eISSN - 1521-3757
pISSN - 0044-8249
DOI - 10.1002/ange.201505798
Subject(s) - rhodopsin , arrestin , chemistry , biophysics , retinal , micelle , flash photolysis , photochemistry , kinetics , g protein coupled receptor , receptor , biochemistry , biology , organic chemistry , reaction rate constant , physics , quantum mechanics , aqueous solution
Continued activation of the photocycle of the dim‐light receptor rhodopsin leads to the accumulation of all‐ trans ‐retinal in the rod outer segments (ROS). This accumulation can damage the photoreceptor cell. For retinal homeostasis, deactivation processes are initiated in which the release of retinal is delayed. One of these processes involves the binding of arrestin to rhodopsin. Here, the interaction of pre‐activated truncated bovine visual arrestin (Arr Tr ) with rhodopsin in 1,2‐diheptanoyl‐ sn ‐glycero‐3‐phosphocholine (DHPC) micelles is investigated by solution NMR techniques and flash photolysis spectroscopy. Our results show that formation of the rhodopsin–arrestin complex markedly influences partitioning in the decay kinetics of rhodopsin, which involves the simultaneous formation of a meta II and a meta III state from the meta I state. Binding of Arr Tr leads to an increase in the population of the meta III state and consequently to an approximately twofold slower release of all‐ trans ‐retinal from rhodopsin.