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000041922 0247_ $$2DOI$$a10.1039/b410923f
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000041922 041__ $$aeng
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000041922 084__ $$2WoS$$aBiochemistry & Molecular Biology
000041922 084__ $$2WoS$$aBiophysics
000041922 084__ $$2WoS$$aChemistry, Physical
000041922 1001_ $$0P:(DE-HGF)0$$aLaan, W.$$b0
000041922 245__ $$aChromophore composition of a heterologously expressed BLUF-domain
000041922 260__ $$aCambridge$$bRoyal Society of Chemistry$$c2004
000041922 300__ $$a1011 - 1016
000041922 3367_ $$0PUB:(DE-HGF)16$$2PUB:(DE-HGF)$$aJournal Article
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000041922 440_0 $$09703$$aPhotochemical and Photobiological Sciences$$v3$$x1474-905X
000041922 500__ $$aRecord converted from VDB: 12.11.2012
000041922 520__ $$aUpon heterologous expression of the BLUF (for: Blue-Light sensing Using Flavin) domain from AppA, a transcriptional anti-repressor from Rhodobacter sphaeroides, in Escherichia coli, photoactive holo-protein is formed through non-covalent binding of a flavin. Whereas it is generally assumed that FAD is the physiological chromophore of this photo-perception domain in vivo, E. coli can (and does) insert, depending on the growth conditions, all naturally occurring flavins, i.e. riboflavin, FMN and FAD into this protein domain. The nature of the particular flavin bound affects the photochemical- and particularly the fluorescence properties of the N-terminal domain of this photosensory protein.
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000041922 650_2 $$2MeSH$$aBacterial Proteins: chemistry
000041922 650_2 $$2MeSH$$aBacterial Proteins: genetics
000041922 650_2 $$2MeSH$$aBacterial Proteins: radiation effects
000041922 650_2 $$2MeSH$$aCloning, Molecular
000041922 650_2 $$2MeSH$$aEscherichia coli
000041922 650_2 $$2MeSH$$aFlavoproteins: chemistry
000041922 650_2 $$2MeSH$$aFlavoproteins: genetics
000041922 650_2 $$2MeSH$$aFlavoproteins: radiation effects
000041922 650_2 $$2MeSH$$aLight
000041922 650_2 $$2MeSH$$aRecombinant Proteins: chemistry
000041922 650_2 $$2MeSH$$aRecombinant Proteins: radiation effects
000041922 650_2 $$2MeSH$$aRhodobacter sphaeroides
000041922 650_2 $$2MeSH$$aSpectrometry, Fluorescence
000041922 650_2 $$2MeSH$$aSpectroscopy, Fourier Transform Infrared
000041922 650_7 $$00$$2NLM Chemicals$$aAppA protein, Rhodobacter sphaeroides
000041922 650_7 $$00$$2NLM Chemicals$$aBacterial Proteins
000041922 650_7 $$00$$2NLM Chemicals$$aFlavoproteins
000041922 650_7 $$00$$2NLM Chemicals$$aRecombinant Proteins
000041922 650_7 $$2WoSType$$aJ
000041922 7001_ $$0P:(DE-Juel1)VDB37437$$aBednarz, T.$$b1$$uFZJ
000041922 7001_ $$0P:(DE-Juel1)VDB572$$aHeberle, J.$$b2$$uFZJ
000041922 7001_ $$0P:(DE-HGF)0$$aHellingwerf, K.$$b3
000041922 773__ $$0PERI:(DE-600)2072584-X$$a10.1039/b410923f$$gVol. 3, p. 1011 - 1016$$p1011 - 1016$$q3<1011 - 1016$$tPhotochemical & photobiological sciences$$v3$$x1474-905X$$y2004
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000041922 9141_ $$y2004
000041922 915__ $$0StatID:(DE-HGF)0010$$aJCR/ISI refereed
000041922 9201_ $$0I:(DE-Juel1)VDB58$$d31.12.2006$$gIBI$$kIBI-2$$lBiologische Strukturforschung$$x0
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