D. Bhattacharya et al., RADIATION-INDUCED INACTIVATION OF FLAVOCYTOCHROME B(2) IN DILUTE AQUEOUS-SOLUTION, Biochimica et biophysica acta. Protein structure and molecular enzymology, 1250(1), 1995, pp. 1-8
Effect of gamma radiation on flavocytochrome b(2) in dilute aqueous so
lution was studied. A study of the effect of the radiolytically produc
ed inorganic free-radical anions such as I-2(-), BT2- and (SCN)(2)(.-)
on the enzyme activity indicates the involvement of cysteine and tyro
sine residues in the catalytic activity of flavocytochrome b(2). The c
hanges in kinetic parameters, i.e., Michaelis-Menten constant K-m and
maximal velocity V-max, due to irradiation under different conditions
suggest that radiation induced enzyme inactivation is the result of de
struction of active-site residues as well as modification of the subst
rate binding site. Fluorescence studies of unirradiated and irradiated
enzyme reveal that FMN (flavin mononucleotide) is inaccessible to wat
er radicals.