FERRYLMYOGLOBIN-CATALYZED LINOLEIC-ACID PEROXIDATION

The addition of linoleic acid (18:2) to a solution containing oxymyoglobin (MbIIO2), metmyoglobin (MbIII), or metmyoglobin-azide complex (MbIII-N3-) resulted in the formation of a common complex with identical absorption spectral properties. The addition of H2O2 to a MbIII/linoleic acid mixture revealed a spectral profile with λmax at 530 nm and different from that observed in the reaction of MbIII with H2O2 and identical to that of ferrylmyoglobin. This was accompanied by a progressive decrease in the absorption in the visible region, indicating heme degradation during the lipid peroxidation process. The oxidation products of linoleic acid during the MbIII/18:2/H2O2 interaction were assessed by HPLC under anaerobic and aerobic conditions. In both instances, the chromatograms at λ234nm revealed the formation of a main peak with a retention time of 11.1 min, which cochromatographed with a standard of 9-hydroperoxide of linoleic acid. The latter adduct was not degraded by the oxoferryl complex of myoglobin. The conclusions originating from this research are twofold. On the one hand, the identical spectral properties exhibited by the product originating from the reaction of either MbIIO2 or MbIII with linoleic acid bridge the apparent discrepancy between the different reactivities of MbIIO2 and MbIII toward H2O2 and their ability to promote lipid peroxidation. On the other hand, the pattern of oxidation products of linoleic acid observed during the MbIII/H2O2 interaction, i.e., the formation of a 9-hydroperoxide adduct as a major product, points to a specific binding character and a regioselectivity of the oxoferryl complex in the oxidation of unsaturated fatty acids or a catalytic preference for decomposition of the various isomeric hydroperoxides over that of the 9-hydroperoxide. © 1990.