TY  - JOUR
AU  - Laan, W.
AU  - Bednarz, T.
AU  - Heberle, J.
AU  - Hellingwerf, K.
TI  - Chromophore composition of a heterologously expressed BLUF-domain
JO  - Photochemical & photobiological sciences
VL  - 3
SN  - 1474-905X
CY  - Cambridge
PB  - Royal Society of Chemistry
M1  - PreJuSER-41922
SP  - 1011 - 1016
PY  - 2004
N1  - Record converted from VDB: 12.11.2012
AB  - 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.
KW  - Bacterial Proteins: chemistry
KW  - Bacterial Proteins: genetics
KW  - Bacterial Proteins: radiation effects
KW  - Cloning, Molecular
KW  - Escherichia coli
KW  - Flavoproteins: chemistry
KW  - Flavoproteins: genetics
KW  - Flavoproteins: radiation effects
KW  - Light
KW  - Recombinant Proteins: chemistry
KW  - Recombinant Proteins: radiation effects
KW  - Rhodobacter sphaeroides
KW  - Spectrometry, Fluorescence
KW  - Spectroscopy, Fourier Transform Infrared
KW  - AppA protein, Rhodobacter sphaeroides (NLM Chemicals)
KW  - Bacterial Proteins (NLM Chemicals)
KW  - Flavoproteins (NLM Chemicals)
KW  - Recombinant Proteins (NLM Chemicals)
KW  - J (WoSType)
LB  - PUB:(DE-HGF)16
C6  - pmid:15570388
UR  - <Go to ISI:>//WOS:000225406800006
DO  - DOI:10.1039/b410923f
UR  - https://juser.fz-juelich.de/record/41922
ER  -