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000059166 0247_ $$2DOI$$a10.1074/jbc.M608872200
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000059166 084__ $$2WoS$$aBiochemistry & Molecular Biology
000059166 1001_ $$0P:(DE-HGF)0$$aBerndt, A.$$b0
000059166 245__ $$aA Novel Photoreaction Mechanism for the Circadian Blue Light Photoreceptor Drosophila Cryptochrome
000059166 260__ $$aBethesda, Md.$$bSoc.$$c2007
000059166 300__ $$a13011 - 13021
000059166 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000059166 440_0 $$03091$$aJournal of Biological Chemistry$$v282$$x0021-9258
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000059166 520__ $$aCryptochromes are flavoproteins that are evolutionary related to the DNA photolyases but lack DNA repair activity. Drosophila cryptochrome (dCRY) is a blue light photoreceptor that is involved in the synchronization of the circadian clock with the environmental light-dark cycle. Until now, spectroscopic and structural studies on this and other animal cryptochromes have largely been hampered by difficulties in their recombinant expression. We have therefore established an expression and purification scheme that enables us to purify mg amounts of monomeric dCRY from Sf21 insect cell cultures. Using UV-visible spectroscopy, mass spectrometry, and reversed phase high pressure liquid chromatography, we show that insect cell-purified dCRY contains flavin adenine dinucleotide in its oxidized state (FAD(ox)) and residual amounts of methenyltetrahydrofolate. Upon blue light irradiation, dCRY undergoes a reversible absorption change, which is assigned to the conversion of FAD(ox) to the red anionic FAD(.) radical. Our findings lead us to propose a novel photoreaction mechanism for dCRY, in which FAD(ox) corresponds to the ground state, whereas the FAD(.) radical represents the light-activated state that mediates resetting of the Drosophila circadian clock.
000059166 536__ $$0G:(DE-Juel1)FUEK409$$2G:(DE-HGF)$$aFunktion und Dysfunktion des Nervensystems$$cP33$$x0
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000059166 650_2 $$2MeSH$$aAnimals
000059166 650_2 $$2MeSH$$aCell Line
000059166 650_2 $$2MeSH$$aCircadian Rhythm
000059166 650_2 $$2MeSH$$aCryptochromes
000059166 650_2 $$2MeSH$$aDNA Repair
000059166 650_2 $$2MeSH$$aDeoxyribodipyrimidine Photo-Lyase: chemistry
000059166 650_2 $$2MeSH$$aDrosophila: chemistry
000059166 650_2 $$2MeSH$$aDrosophila: metabolism
000059166 650_2 $$2MeSH$$aDrosophila Proteins: chemistry
000059166 650_2 $$2MeSH$$aDrosophila Proteins: metabolism
000059166 650_2 $$2MeSH$$aFlavin-Adenine Dinucleotide: chemistry
000059166 650_2 $$2MeSH$$aFlavin-Adenine Dinucleotide: metabolism
000059166 650_2 $$2MeSH$$aFlavoproteins: chemistry
000059166 650_2 $$2MeSH$$aFlavoproteins: metabolism
000059166 650_2 $$2MeSH$$aOxidation-Reduction
000059166 650_2 $$2MeSH$$aPhotochemistry
000059166 650_2 $$2MeSH$$aPhotoreceptor Cells, Invertebrate: chemistry
000059166 650_2 $$2MeSH$$aPhotoreceptor Cells, Invertebrate: metabolism
000059166 650_7 $$00$$2NLM Chemicals$$aCryptochromes
000059166 650_7 $$00$$2NLM Chemicals$$aDrosophila Proteins
000059166 650_7 $$00$$2NLM Chemicals$$aFlavoproteins
000059166 650_7 $$0146-14-5$$2NLM Chemicals$$aFlavin-Adenine Dinucleotide
000059166 650_7 $$0EC 4.1.99.3$$2NLM Chemicals$$aDeoxyribodipyrimidine Photo-Lyase
000059166 650_7 $$2WoSType$$aJ
000059166 7001_ $$0P:(DE-Juel1)VDB16784$$aKottke, T.$$b1$$uFZJ
000059166 7001_ $$0P:(DE-HGF)0$$aBreitkreuz, H.$$b2
000059166 7001_ $$0P:(DE-HGF)0$$aDvorsky, R.$$b3
000059166 7001_ $$0P:(DE-HGF)0$$aHennig, S.$$b4
000059166 7001_ $$0P:(DE-HGF)0$$aAlexander, M.$$b5
000059166 7001_ $$0P:(DE-HGF)0$$aWolf, E.$$b6
000059166 773__ $$0PERI:(DE-600)1474604-9$$a10.1074/jbc.M608872200$$gVol. 282, p. 13011 - 13021$$p13011 - 13021$$q282<13011 - 13021$$tThe @journal of biological chemistry$$v282$$x0021-9258$$y2007
000059166 8567_ $$uhttp://dx.doi.org/10.1074/jbc.M608872200
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