Initial characterization of the primary photochemistry of AppA, a blue-light-using flavin adenine dinucleotide-domain containing transcriptional antirepressor protein from Rhodobacter sphaeroides: A key role for reversible intramolecular proton transfer from the flavin adenine dinucleotide chromophore to a conserved tyrosine?
| Autor: | Wouter Laan, Ivo H. M. van Stokkum, Michael A. van der Horst, Klaas J. Hellingwerf |
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| Přispěvatelé: | Molecular Microbial Physiology (SILS, FNWI), Biophysics Photosynthesis/Energy |
| Jazyk: | angličtina |
| Rok vydání: | 2003 |
| Předmět: |
Flavin adenine dinucleotide
Primary (chemistry) Proton biology Stereochemistry Mutagenesis Photoreceptor protein Flavoprotein General Medicine Chromophore biology.organism_classification Photochemistry Biochemistry Rhodobacter sphaeroides chemistry.chemical_compound chemistry Intramolecular force biology.protein Physical and Theoretical Chemistry Blue light BLUF domain |
| Zdroj: | Photochemistry and Photobiology, 78(3), 290-297. Wiley-Blackwell Laan, W, Horst, M A, van Stokkum, I H M & Hellingwerf, K J 2003, ' Initial characterization of the primary photochemistry of AppA, a blue-light-using flavin adenine dinucleotide-domain containing transcriptional antirepressor protein from Rhodobacter sphaeroides: A key role for reversible intramolecular proton transfer from the flavin adenine dinucleotide chromophore to a conserved tyrosine? ', Photochemistry and Photobiology, vol. 78, no. 3, pp. 290-297 . https://doi.org/10.1562/0031-8655(2003)078<0290:ICOTPP>2.0.CO;2 |
| ISSN: | 0031-8655 |
| Popis: | The flavin adenine dinucleotide (FAD)-containing photoreceptor protein AppA (in which the FAD is bound to a novel so-called BLUF domain) from the purple nonsulfur bacterium Rhodobacter sphaeroides was previously shown to be photoactive by the formation of a slightly redshifted long-lived intermediate that is thought to be the signaling state. In this study, we provide further characterization of the primary photochemistry of this photoreceptor protein using UV-Vis and Fourier-transform infrared spectroscopy, pH measurements and site-directed mutagenesis. Available evidence indicates that the FAD chromophore of AppA may be protonated in the receptor state, and that it becomes exposed to solvent in the signaling state. Furthermore, experimental data lead to the suggestion that intramolecular proton transfer (that may involve [anionic] Tyr-17) forms the basis for the stabilization of the signaling state. |
| Databáze: | OpenAIRE |
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