Chromophore composition of a heterologously expressed BLUF-domain

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...

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Bibliographic Details
Published in:Photochemical & photobiological sciences 2004-11, Vol.3 (11-12), p.1011-1016
Main Authors: Laan, Wouter, Bednarz, Teresa, Heberle, Joachim, Hellingwerf, Klaas J
Format: Article
Language:English
Subjects:
Bacterial Proteins - chemistry
Bacterial Proteins - genetics
Bacterial Proteins - radiation effects
Cloning, Molecular
Escherichia coli
Flavoproteins - chemistry
Flavoproteins - genetics
Flavoproteins - radiation effects
Light
Recombinant Proteins - chemistry
Recombinant Proteins - radiation effects
Rhodobacter sphaeroides
Spectrometry, Fluorescence
Spectroscopy, Fourier Transform Infrared
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Summary: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.
ISSN:1474-905X
1474-9092
DOI:10.1039/b410923f