LIGHT-INDUCED BINDING OF RIBOFLAVIN TO LYSOZYME
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Date
1977
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Abstract
Photodynamic inactivation of lysozyme in air saturated H2O and D2O (phosphate buffer 0.05 M, pH 7.0) in the presence of methylene blue and riboflavin was studied. When H2O was replaced by D2O a great increase in rate of photoinactivation of lysozyme was observed. Photooxidation was inhibited by singlet oxygen quenchers like NaN3, and these reactions may have occurred via a singlet oxygen mechanism. Riboflavin was strongly bound to the enzyme as a result of illumination. A higher quantum was observed when riboflavin was used, although this dye was bleached during irradiation.