Journal Article

PreJuSER-41922

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Chromophore composition of a heterologously expressed BLUF-domain

Laan, W. ; Bednarz, T.FZJ* ; Heberle, J.FZJ* ; Hellingwerf, K.

2004
Royal Society of Chemistry Cambridge

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Please use a persistent id in citations: doi:10.1039/b410923f

Abstract: 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.

Keyword(s): Bacterial Proteins: chemistry (MeSH) ; Bacterial Proteins: genetics (MeSH) ; Bacterial Proteins: radiation effects (MeSH) ; Cloning, Molecular (MeSH) ; Escherichia coli (MeSH) ; Flavoproteins: chemistry (MeSH) ; Flavoproteins: genetics (MeSH) ; Flavoproteins: radiation effects (MeSH) ; Light (MeSH) ; Recombinant Proteins: chemistry (MeSH) ; Recombinant Proteins: radiation effects (MeSH) ; Rhodobacter sphaeroides (MeSH) ; Spectrometry, Fluorescence (MeSH) ; Spectroscopy, Fourier Transform Infrared (MeSH) ; AppA protein, Rhodobacter sphaeroides ; Bacterial Proteins ; Flavoproteins ; Recombinant Proteins ; J

Note: Record converted from VDB: 12.11.2012

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Contributing Institute(s):

1. Biologische Strukturforschung (IBI-2)

Research Program(s):

1. Neurowissenschaften (L01)

Appears in the scientific report 2004

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