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Singlet oxygen formation by a peroxidase ec 1.11.1.7 hydrogen per oxide and halide system



Singlet oxygen formation by a peroxidase ec 1.11.1.7 hydrogen per oxide and halide system



European Journal of Biochemistry 93(2): 323-332



Evidence for singlet oxygen formation was obtained for the lactoperoxidase [EC 1.11.1.4], H2O2 and bromide system by monitoring 2,3-diphenylfuran and diphenylisobenzofuran oxidation, O2 evolution, and chemiluminescence. This could provide an explanation for the [tumor cell] cytotoxic and microbicidal activity of peroxidases and polymorphonuclear leukocytes. Evidence for singlet oxygen formation included the following: chemiluminescence accompanying the enzymic reaction was doubled in a deuterated buffer and inhibited by singlet oxygen traps; the singlet oxygen traps, diphenylfuran and diphenylisobenzofuran, were oxidized to their known singlet oxygen oxidation products in the presence of lactoperoxidase, H2O2 and bromide; the rate of oxidation of diphenylfuran and diphenylisobenzofuran was inhibited when monitored in the presence of known singlet oxygen traps or quenchers; oxygen evolution from the enzymic reaction was inhibited by singlet oxygen traps but not be singlet oxygen quenchers; and the traps or quenchers which were effective inhibitors in the experiments above did not inhibit peroxidase activity, were competitive peroxidase substrates and did not react with the hypobromite intermediate since they did not inhibit H2O2 consumption by the enzyme. Using these criteria, various biological molecules were tested for their reactivity with singlet oxygen. By studying their effect on oxygen release by the enzymic reaction, it could be ascertained whether they were acting as singlet oxygen traps or quenchers.

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