title: Investigation of binding properties of umbelliferone (7hydroxycoumarin) to lysozyme.
abstract: The binding interaction of lysozyme and umbelliferone (7hydroxcoumarin, 7HC) was investigated by UV-vis absorption and fluorescence quenching. It was obtained from fluorescence spectra that the fluorescence quenching of lysozyme by 7HC was probably a result of the formation of lysozyme-7HC complex and binding parameters were determined according to the Stern-Volmer equation. The effects of various common metal ions on the binding were also studied. The thermodynamic parameters were calculated at different temperatures which indicated that hydrophobic interaction. The binding distance (r) between the donor (lysozyme) and the acceptor (7HC) was 3.81 nm based on the Förster theory of non-radioactive resonance energy transfer.
authors.affiliation: Department of Chemistry, Hacettepe University, 06800, Ankara, Turkey. gokoglu@hacettepe.edu.tr
authors.forename: Elmas
authors.initials: E
authors.lastname: Gök
mesh_terms: D004735:Energy Transfer; D057927:Hydrophobic and Hydrophilic Interactions; D009113:Muramidase / Q000378:metabolism*; D011485:Protein Binding; D013050:Spectrometry, Fluorescence / Q000379:methods*; D013056:Spectrophotometry, Ultraviolet; D013816:Thermodynamics; D014468:Umbelliferones / Q000378:metabolism*
chemical_list: D014468:Umbelliferones; C031477:7-hydroxycoumarin; D009113:Muramidase