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000051338 0247_ $$2DOI$$a10.1021/bi051964b
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000051338 084__ $$2WoS$$aBiochemistry & Molecular Biology
000051338 1001_ $$0P:(DE-Juel1)VDB16784$$aKottke, T.$$b0$$uFZJ
000051338 245__ $$aBlue-Light-Induced Changes in Arabidopsis Cryptochrome 1 Probed by FTIR Difference Spectroscopy
000051338 260__ $$aColumbus, Ohio$$bAmerican Chemical Society$$c2006
000051338 300__ $$a2472 - 2479
000051338 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000051338 440_0 $$0798$$aBiochemistry$$v45$$x0006-2960
000051338 500__ $$aRecord converted from VDB: 12.11.2012
000051338 520__ $$aCryptochromes are blue-light photoreceptors that regulate a variety of responses in animals and plants, including circadian entrainment in Drosophila and photomorphogenesis in Arabidopsis. They comprise a photolyase homology region (PHR) of about 500 amino acids and a C-terminal extension of varying length. In the PHR domain, flavin adenine dinucleotide (FAD) is noncovalently bound. The presence of a second chromophore, such as methenyltetrahydrofolate, in animal and plant cryptochromes is still under debate. Arabidopsis cryptochrome 1 (CRY1) has been intensively studied with regard to function and interaction of the protein in vivo and in vitro. However, little is known about the pathway from light absorption to signal transduction on the molecular level. We investigated the full-length CRY1 protein by Fourier transform infrared (FTIR) and UV/vis difference spectroscopy. Starting from the fully oxidized state of the chromophore FAD, a neutral flavoprotein radical is formed upon illumination in the absence of any exogenous electron donor. A preliminary assignment of the chromophore bands is presented. The FTIR difference spectrum reveals only moderate changes in secondary structure of the apoprotein in response to the photoreduction of the chromophore. Deprotonation of an aspartic or glutamic acid, probably D396, accompanies radical formation, as is deduced from the negative band at 1734 cm(-)(1) in D(2)O. The main positive band at 1524 cm(-)(1) in the FTIR spectrum shows a strong shift to lower frequencies as compared to other flavoproteins. Together with the unusual blue-shift of the absorption in the visible range to 595 nm, this clearly distinguishes the radical form of CRY1 from those of structurally highly homologous DNA photolyases. As a consequence, the direct comparison of cryptochrome to photolyase in terms of photoreactivity and mechanism has to be made with caution.
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000051338 650_2 $$2MeSH$$aArabidopsis Proteins: chemistry
000051338 650_2 $$2MeSH$$aCryptochromes
000051338 650_2 $$2MeSH$$aCrystallography, X-Ray
000051338 650_2 $$2MeSH$$aDeoxyribodipyrimidine Photo-Lyase: chemistry
000051338 650_2 $$2MeSH$$aDeoxyribodipyrimidine Photo-Lyase: metabolism
000051338 650_2 $$2MeSH$$aEscherichia coli: metabolism
000051338 650_2 $$2MeSH$$aFlavins: metabolism
000051338 650_2 $$2MeSH$$aFlavoproteins: chemistry
000051338 650_2 $$2MeSH$$aFlavoproteins: metabolism
000051338 650_2 $$2MeSH$$aLight
000051338 650_2 $$2MeSH$$aModels, Molecular
000051338 650_2 $$2MeSH$$aSignal Transduction: physiology
000051338 650_2 $$2MeSH$$aSpectrophotometry, Ultraviolet
000051338 650_2 $$2MeSH$$aSpectroscopy, Fourier Transform Infrared: methods
000051338 650_2 $$2MeSH$$aStructural Homology, Protein
000051338 650_7 $$00$$2NLM Chemicals$$aArabidopsis Proteins
000051338 650_7 $$00$$2NLM Chemicals$$aCryptochromes
000051338 650_7 $$00$$2NLM Chemicals$$aFlavins
000051338 650_7 $$00$$2NLM Chemicals$$aFlavoproteins
000051338 650_7 $$0EC 4.1.99.3$$2NLM Chemicals$$aDeoxyribodipyrimidine Photo-Lyase
000051338 650_7 $$2WoSType$$aJ
000051338 7001_ $$0P:(DE-HGF)0$$aAhmad, M.$$b1
000051338 7001_ $$0P:(DE-HGF)0$$aBatschauer, A.$$b2
000051338 7001_ $$0P:(DE-Juel1)VDB572$$aHeberle, J.$$b3$$uFZJ
000051338 773__ $$0PERI:(DE-600)1472258-6$$a10.1021/bi051964b$$gVol. 45, p. 2472 - 2479$$p2472 - 2479$$q45<2472 - 2479$$tBiochemistry$$v45$$x0006-2960$$y2006
000051338 8567_ $$uhttp://hdl.handle.net/2128/714$$uhttp://dx.doi.org/10.1021/bi051964b
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000051338 9201_ $$0I:(DE-Juel1)VDB58$$d31.12.2006$$gIBI$$kIBI-2$$lBiologische Strukturforschung$$x0
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