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

Visser, Antonie J. W. G.; Hoek, Arie van; Visser, Nina V.; Lee, Yongho; Ghisla, Sandro

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

Dateien

Time_resolved_fluorescence_study_of_the_dissociation_of_FMN_from_the_yellow_fluorescence_protein_from_Vibrio_fischeri.pdfGröße: 651.83 KBDownloads: 445

Datum

1997

Autor:innen

Visser, Antonie J. W. G.

Hoek, Arie van

Visser, Nina V.

Lee, Yongho

Ghisla, Sandro

Open Access-Veröffentlichung

Open Access Green

Sammlungen

Biologie

Publikationstyp

Zeitschriftenartikel

Publikationsstatus

Published

Erschienen in

Photochemistry and Photobiology. 1997, 65(3), pp. 570-575. ISSN 0031-8655. eISSN 1751-1097. Available under: doi: 10.1111/j.1751-1097.1997.tb08607.x

Zusammenfassung

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).

Fachgebiet (DDC)

570 Biowissenschaften, Biologie

Zitieren

ISO 690

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. 1997, 65(3), pp. 570-575. ISSN 0031-8655. eISSN 1751-1097. Available under: doi: 10.1111/j.1751-1097.1997.tb08607.x

BibTex

@article{Visser1997Timer-8008,
  year={1997},
  doi={10.1111/j.1751-1097.1997.tb08607.x},
  title={Time-resolved fluorescence study of the dissociation of FMN from the yellow fluorescence protein from Vibrio fischeri},
  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}
}

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    <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>
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