Possible mechanism of oxygen activation in linoleate peroxidation by fusarium lipoxygenase.

Abstract

The Oxygen activating mechanism of Fusarium lipoxygenase, a heme-containing dioxygenase, was studied. The enzyme did not require any cofactors, such as H2O2, however, both superoxide dismutase and catalase inhibited linoleate peroxidation by Fusarium lipoxygenase. A low concentration of H2O2 caused a distinct acceleration in enzymatic peroxidation. These results indicate that both O2− and H2O2 are produced as essential intermediates of oxygen activation during formation of linoleate hydroperoxides by Fusarium lipoxygenase. This peroxidation reaction was also prevented by scavengers of singlet oxygen (1O2), but not by scavengers of hydroxy 1 radical (OH). Generation of O2− in the enzyme reaction was detected by its ability to oxidize epinephrine to adrenochrome. Moreover, the rate of peroxide formation was greater in the D2O than in the H2O buffer system. These results suggest that the Haber–Weiss reaction (O2−+H2O2→OH−+OH·+1O2) is taking part in linoleate peroxidation by Fusarium lipoxygenase, and the 1O2...