Influence of Arrestin on the Photodecay of Bovine Rhodopsin |
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| Authors: | Deep Chatterjee Carl Elias Eckert Dr Chavdar Slavov Dr Krishna Saxena Dr Boris Fürtig Prof?Dr Charles R Sanders Prof?Dr Vsevolod V Gurevich Prof?Dr Josef Wachtveitl Prof?Dr Harald Schwalbe |
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| Institution: | 1. Institute of Organic Chemistry and Chemical Biology, Center of Biomolecular Magnetic Resonance (BMRZ), Goethe University Frankfurt/Main, Max‐von‐Laue‐Strasse 7, 60438 Frankfurt am Main (Germany);2. Institute of Physical and Theoretical Chemistry, Goethe University Frankfurt/Main, Max‐von‐Laue‐Strasse 7, 60438 Frankfurt am Main (Germany);3. Department of Biochemistry, Center for Structural Biology, Institute of Chemical Biology, Vanderbilt University School of Medicine, Nashville, TN 37232 (USA);4. Department of Pharmacology, Vanderbilt University School of Medicine, Nashville, TN 37232 (USA) |
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| Abstract: | 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 (ArrTr) 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 ArrTr 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. |
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| Keywords: | arrestin NMR spectroscopy retinal regeneration rhodopsin UV/Vis spectroscopy |
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