Thermodynamics of association of 8-substituted riboflavins with egg white riboflavin binding protein.
Association constants of 14 species of riboflavin derivatives with hen egg-white riboflavin binding protein were measured by a fluorometric titration method using flavin and protein fluorescence in a temperature range of 10--42 degrees C. The derivatives were riboflavins whose 8-CH3 group was substituted with alkylamino, alkyloxy, halogen or hydrogen. The flavin derivatives were classified into four groups, i.e., RR'N, HRN, RO, and halogen, on the basis of the linear relation between enthalpy and entropy changes (linear free energy relationship), and from the chemical structures of the 8-substituents. The relation between the entropy change and the bulkiness of 8-substituents suggested burying of the substituents in a cavity of the protein, and provided an indication of the size of the substituent-accepting cavity. The relation also suggested an electric repulsion between halogen substituents and the binding site. A very good correlation was found between the constant term of the linear free energy relation and the wavelength of the visible absorption peak of flavins, and this correlation suggested the electronic nature of the flavin-protein interaction.
D002352:Carrier Proteins / Q000032:analysis*; D004527:Egg Proteins / Q000032:analysis*; D004529:Egg White; D004563:Electrochemistry; D026901:Membrane Transport Proteins; D011485:Protein Binding; D012256:Riboflavin / Q000031:analogs & derivatives* / Q000032:analysis; D013816:Thermodynamics
D002352:Carrier Proteins; D004527:Egg Proteins; D026901:Membrane Transport Proteins; C019079:riboflavin-binding protein; D012256:Riboflavin