001     41922
005     20200402205822.0
024 7 _ |2 pmid
|a pmid:15570388
024 7 _ |2 DOI
|a 10.1039/b410923f
024 7 _ |2 WOS
|a WOS:000225406800006
037 _ _ |a PreJuSER-41922
041 _ _ |a eng
082 _ _ |a 620
084 _ _ |2 WoS
|a Biochemistry & Molecular Biology
084 _ _ |2 WoS
|a Biophysics
084 _ _ |2 WoS
|a Chemistry, Physical
100 1 _ |a Laan, W.
|b 0
|0 P:(DE-HGF)0
245 _ _ |a Chromophore composition of a heterologously expressed BLUF-domain
260 _ _ |a Cambridge
|b Royal Society of Chemistry
|c 2004
300 _ _ |a 1011 - 1016
336 7 _ |a Journal Article
|0 PUB:(DE-HGF)16
|2 PUB:(DE-HGF)
336 7 _ |a Output Types/Journal article
|2 DataCite
336 7 _ |a Journal Article
|0 0
|2 EndNote
336 7 _ |a ARTICLE
|2 BibTeX
336 7 _ |a JOURNAL_ARTICLE
|2 ORCID
336 7 _ |a article
|2 DRIVER
440 _ 0 |a Photochemical and Photobiological Sciences
|x 1474-905X
|0 9703
|v 3
500 _ _ |a Record converted from VDB: 12.11.2012
520 _ _ |a Upon 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.
536 _ _ |a Neurowissenschaften
|c L01
|2 G:(DE-HGF)
|0 G:(DE-Juel1)FUEK255
|x 0
588 _ _ |a Dataset connected to Web of Science, Pubmed
650 _ 2 |2 MeSH
|a Bacterial Proteins: chemistry
650 _ 2 |2 MeSH
|a Bacterial Proteins: genetics
650 _ 2 |2 MeSH
|a Bacterial Proteins: radiation effects
650 _ 2 |2 MeSH
|a Cloning, Molecular
650 _ 2 |2 MeSH
|a Escherichia coli
650 _ 2 |2 MeSH
|a Flavoproteins: chemistry
650 _ 2 |2 MeSH
|a Flavoproteins: genetics
650 _ 2 |2 MeSH
|a Flavoproteins: radiation effects
650 _ 2 |2 MeSH
|a Light
650 _ 2 |2 MeSH
|a Recombinant Proteins: chemistry
650 _ 2 |2 MeSH
|a Recombinant Proteins: radiation effects
650 _ 2 |2 MeSH
|a Rhodobacter sphaeroides
650 _ 2 |2 MeSH
|a Spectrometry, Fluorescence
650 _ 2 |2 MeSH
|a Spectroscopy, Fourier Transform Infrared
650 _ 7 |0 0
|2 NLM Chemicals
|a AppA protein, Rhodobacter sphaeroides
650 _ 7 |0 0
|2 NLM Chemicals
|a Bacterial Proteins
650 _ 7 |0 0
|2 NLM Chemicals
|a Flavoproteins
650 _ 7 |0 0
|2 NLM Chemicals
|a Recombinant Proteins
650 _ 7 |a J
|2 WoSType
700 1 _ |a Bednarz, T.
|b 1
|u FZJ
|0 P:(DE-Juel1)VDB37437
700 1 _ |a Heberle, J.
|b 2
|u FZJ
|0 P:(DE-Juel1)VDB572
700 1 _ |a Hellingwerf, K.
|b 3
|0 P:(DE-HGF)0
773 _ _ |a 10.1039/b410923f
|g Vol. 3, p. 1011 - 1016
|p 1011 - 1016
|q 3<1011 - 1016
|0 PERI:(DE-600)2072584-X
|t Photochemical & photobiological sciences
|v 3
|y 2004
|x 1474-905X
909 C O |o oai:juser.fz-juelich.de:41922
|p VDB
913 1 _ |k L01
|v Neurowissenschaften
|l Funktion und Dysfunktion des Nervensystems
|b Leben
|0 G:(DE-Juel1)FUEK255
|x 0
914 1 _ |y 2004
915 _ _ |0 StatID:(DE-HGF)0010
|a JCR/ISI refereed
920 1 _ |k IBI-2
|l Biologische Strukturforschung
|d 31.12.2006
|g IBI
|0 I:(DE-Juel1)VDB58
|x 0
970 _ _ |a VDB:(DE-Juel1)58219
980 _ _ |a VDB
980 _ _ |a ConvertedRecord
980 _ _ |a journal
980 _ _ |a I:(DE-Juel1)ISB-2-20090406
980 _ _ |a UNRESTRICTED
980 _ _ |a I:(DE-Juel1)ICS-6-20110106
981 _ _ |a I:(DE-Juel1)IBI-7-20200312
981 _ _ |a I:(DE-Juel1)ISB-2-20090406
981 _ _ |a I:(DE-Juel1)ICS-6-20110106


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