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Time-resolved fluorescence study of the dissociation of FMN from the yellow fluorescence protein from Vibrio fischeri

Time-resolved fluorescence study of the dissociation of FMN from the yellow fluorescence protein from Vibrio fischeri

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VISSER, Antonie J. W. G., Arie van HOEK, Nina V. VISSER, Yongho LEE, Sandro GHISLA, 1997. Time-resolved fluorescence study of the dissociation of FMN from the yellow fluorescence protein from Vibrio fischeri. In: Photochemistry and Photobiology. 65(3), pp. 570-575. ISSN 0031-8655. eISSN 1751-1097

@article{Visser1997Time--8008, title={Time-resolved fluorescence study of the dissociation of FMN from the yellow fluorescence protein from Vibrio fischeri}, year={1997}, doi={10.1111/j.1751-1097.1997.tb08607.x}, number={3}, volume={65}, issn={0031-8655}, journal={Photochemistry and Photobiology}, pages={570--575}, author={Visser, Antonie J. W. G. and Hoek, Arie van and Visser, Nina V. and Lee, Yongho and Ghisla, Sandro} }

<rdf:RDF xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/8008"> <dc:contributor>Lee, Yongho</dc:contributor> <dc:creator>Hoek, Arie van</dc:creator> <dcterms:issued>1997</dcterms:issued> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:39:14Z</dc:date> <dc:language>eng</dc:language> <dc:rights>deposit-license</dc:rights> <dc:contributor>Ghisla, Sandro</dc:contributor> <dc:creator>Ghisla, Sandro</dc:creator> <dcterms:abstract xml:lang="eng">Time-resolved fluorescence spectroscopy of the flavin mononucleotide (FMN) prosthetic group of the yellow fluorescence protein (YFP) from Vibrio fischeri has provided quantitative, thermodynamic information on the FMN-apoYFP equilibrium in aqueous buffer. In diluted aqueous solution two fluorescent species could be identified by distinct fluorescence lifetimes and rotational correlation times originating from free- and protein-bound FMN. Quantitation of the amounts of free and bound FMN in progressively larger dilutions of YFP in aqueous buffer yielded a dissociation constant of 0.40 fJ.M for the FMN-apoprotein complex at 20°C. The single fluorescence lifetime of YFP-bound FMN is very long (7.6 ns at 20°C), suggesting a binding environment in which maximal emission is provided commensurate with its function as a bioluminescent emitter. The single correlation time of 14.8 ns (20°C) is in agreement with a rigid binding site that rotates together with the whole, hydrated protein. Using a different technique we have obtained the same results as reported by others (G. Sirokman, T. Wilson and J. W. Hastings, Biochemistry 34, 13074-13081, 1995; V. N. Petushkov, B. G. Gibson and J. Lee, Biochem.Biophys. Res. Commun. 211,774-779,1995).</dcterms:abstract> <dcterms:title>Time-resolved fluorescence study of the dissociation of FMN from the yellow fluorescence protein from Vibrio fischeri</dcterms:title> <dc:contributor>Hoek, Arie van</dc:contributor> <dc:format>application/pdf</dc:format> <dcterms:bibliographicCitation>First publ. in: Photochemistry and Photobiology 65 (1997), 3, pp. 570-575</dcterms:bibliographicCitation> <dc:creator>Lee, Yongho</dc:creator> <dc:contributor>Visser, Nina V.</dc:contributor> <dc:contributor>Visser, Antonie J. W. G.</dc:contributor> <dcterms:rights rdf:resource="https://creativecommons.org/licenses/by-nc-nd/2.0/legalcode"/> <bibo:uri rdf:resource="http://kops.uni-konstanz.de/handle/123456789/8008"/> <dc:creator>Visser, Antonie J. W. G.</dc:creator> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2011-03-24T17:39:14Z</dcterms:available> <dc:creator>Visser, Nina V.</dc:creator> </rdf:Description> </rdf:RDF>

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