Chromophore composition of a heterologously expressed BLUF-domain
| Autor: | Joachim Heberle, Teresa Bednarz, Klaas J. Hellingwerf, Wouter Laan |
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| Přispěvatelé: | Molecular Microbial Physiology (SILS, FNWI) |
| Jazyk: | angličtina |
| Rok vydání: | 2004 |
| Předmět: |
biology
Flavoproteins Light Protein domain Flavoprotein Riboflavin Flavin group Rhodobacter sphaeroides Chromophore biology.organism_classification Recombinant Proteins Spectrometry Fluorescence Biochemistry Bacterial Proteins Spectroscopy Fourier Transform Infrared biology.protein Escherichia coli heterocyclic compounds Heterologous expression Physical and Theoretical Chemistry Cloning Molecular BLUF domain |
| Zdroj: | Photochemical & Photobiological Sciences, 3(11-12), 1011-1016. Royal Society of Chemistry |
| ISSN: | 1474-905X |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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