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000005186 0247_ $$2DOI$$a10.1111/j.1751-1097.2008.00517.x
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000005186 084__ $$2WoS$$aBiochemistry & Molecular Biology
000005186 084__ $$2WoS$$aBiophysics
000005186 1001_ $$0P:(DE-HGF)0$$aYanamala, N.$$b0
000005186 245__ $$apH-dependent Interaction of Rhodopsin with Cyanidin-3-glucoside. 1. Structural Aspects
000005186 260__ $$aMalden, Mass.$$bWiley-Blackwell$$c2009
000005186 300__ $$a454 - 462
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000005186 440_0 $$015281$$aPhotochemistry and Photobiology$$v85$$x0031-8655$$y2
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000005186 520__ $$aAnthocyanins are a class of phytochemicals that confer color to flowers, fruits, vegetables and leaves. They are part of our regular diet and serve as dietary supplements because of numerous health benefits, including improved vision. Recent studies have shown that the anthocyanin cyanidin-3-O-glucoside (C3G) increased regeneration of the dim-light photoreceptor rhodopsin (Matsumoto et al. [2003] J. Agric. Food Chem., 51, 3560-3563). In an accompanying study (Yanamala et al. [2009] Photochem. Photobiol.), we show that C3G directly binds to rhodopsin in a pH-dependent manner. In this study, we investigated the functional consequences of C3G binding to rhodopsin. As observed previously in rod outer segments, regeneration of purified rhodopsin in detergent micelles is also accelerated in the presence of C3G. Thermal denaturation and stability studies using circular dichroism, fluorescence and UV/visible absorbance spectroscopy show that C3G exerts a destabilizing effect on rhodopsin structure while it only modestly alters G-protein activation and the rates at which the light-activated Metarhodopsin II state decays to opsin and free retinal. These results indicate that the mechanism of C3G-enhanced regeneration may be based on changes in opsin structure promoting access to the retinal binding pocket.
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000005186 650_2 $$2MeSH$$aAnimals
000005186 650_2 $$2MeSH$$aAnthocyanins: chemistry
000005186 650_2 $$2MeSH$$aAnthocyanins: metabolism
000005186 650_2 $$2MeSH$$aCattle
000005186 650_2 $$2MeSH$$aEnzyme Activation
000005186 650_2 $$2MeSH$$aGTP-Binding Proteins: metabolism
000005186 650_2 $$2MeSH$$aGlucosides: chemistry
000005186 650_2 $$2MeSH$$aGlucosides: metabolism
000005186 650_2 $$2MeSH$$aHydrogen-Ion Concentration
000005186 650_2 $$2MeSH$$aProtein Binding
000005186 650_2 $$2MeSH$$aProtein Structure, Secondary
000005186 650_2 $$2MeSH$$aRhodopsin: chemistry
000005186 650_2 $$2MeSH$$aRhodopsin: isolation & purification
000005186 650_2 $$2MeSH$$aRhodopsin: metabolism
000005186 650_7 $$00$$2NLM Chemicals$$aAnthocyanins
000005186 650_7 $$00$$2NLM Chemicals$$aGlucosides
000005186 650_7 $$07084-24-4$$2NLM Chemicals$$acyanidin 3-O-glucoside
000005186 650_7 $$09009-81-8$$2NLM Chemicals$$aRhodopsin
000005186 650_7 $$0EC 3.6.1.-$$2NLM Chemicals$$aGTP-Binding Proteins
000005186 650_7 $$2WoSType$$aJ
000005186 7001_ $$0P:(DE-HGF)0$$aTirupula, K.C.$$b1
000005186 7001_ $$0P:(DE-Juel1)VDB86778$$aBalem, F.$$b2$$uFZJ
000005186 7001_ $$0P:(DE-Juel1)VDB44599$$aKlein-Seetharaman, J.$$b3$$uFZJ
000005186 773__ $$0PERI:(DE-600)2048860-9$$a10.1111/j.1751-1097.2008.00517.x$$gVol. 85, p. 454 - 462$$n2$$p454 - 462$$q85<454 - 462$$tPhotochemistry and photobiology$$v85$$x0031-8655$$y2009
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000005186 9201_ $$0I:(DE-Juel1)ISB-2-20090406$$d31.12.2010$$gISB$$kISB-2$$lMolekulare Biophysik$$x0
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