Rate constants studies of the dye-sensitized photoinactivation of lysozyme.
The rate constants for the photodynamic inactivation of hen egg-white lysozyme at different temperatures were studied. Arrhenius plots of the methylene blue sensitized photo-inactivation of lysozyme gave an experimental activation energy of 7.5 kcal/mol. The rate constants for the photodynamic inactivation of lysozyme in the presence of riboflavin decreased almost linearly in the temperature range 4-38 degrees C. The photosensitized oxidation of lysozyme at -20 degrees C in freezing and non-freezing solvents was possible only in the presence of riboflavin. The effect of dye concentration on the quantum yield and rate constant for the photodynamic inactivation of lysozyme was examined. The quantum yields were lower when the concentrations of methylene blue used were low, and increased on increasing dye concentration, getting to a maximum and then declined at higher dye concentrations. It was found that in the case of riboflavin sensitized photo-inactivation of lysozyme both the rate constant and the quantum yield increased as the dye concentration increased. No maximum was observed over the range of dye concentrations studied. A new mechanism is postulated for the photodynamic action of lysozyme in the presence of riboflavin.
D055598:Chemical Phenomena; D002621:Chemistry; D007700:Kinetics; D008027:Light; D008751:Methylene Blue; D009113:Muramidase / Q000528:radiation effects*; D010084:Oxidation-Reduction; D012256:Riboflavin; D013696:Temperature
D009113:Muramidase; D008751:Methylene Blue; D012256:Riboflavin