Desferrioxamine as an electron donor. Inhibition of membranal lipid peroxidation initiated by H2O2-activated metmyoglobin and other peroxidizing systems.
Desferrioxamine (DFO) involvement in several peroxidative systems was studied. These systems included: a) membranal lipid peroxidation initiated by H2O2-activated metmyoglobin (or methemoglobin); b) phenol-red oxidation by activated metmyoglobin or horseradish peroxidase (HRP): c) beta-carotene-linoleate couple oxidation stimulated by lipoxygenase or hemin. Desferrioxamine was found to inhibit all these systems but not ferrioxamine (FO). Phenol-red oxidation by H2O2-horseradish peroxidase was inhibited competitively with DFO. Kinetic studies using the spectra changes in the Soret region of metmyoglobin suggest a mechanism by which H2O2 reacts with the iron-heme to form an intermediate of oxy-ferryl myoglobin that subsequently reacts with DFO to return the activated compound to the resting state. These activities of DFO resemble the reaction of other electron donors.
Kanner
J
J
Dept. of Food Science, Agricultural Research Organization, Bet Dagan, Israel.
Harel
S
S
D002462:Cell Membrane / Q000378:metabolism; D003300:Copper / Q000494:pharmacology; D003676:Deferoxamine / Q000494:pharmacology*; D004492:Edetic Acid / Q000494:pharmacology; D004583:Electrons; D006420:Hemeproteins / Q000502:physiology*; D006735:Horseradish Peroxidase / Q000494:pharmacology; D006861:Hydrogen Peroxide / Q000494:pharmacology; D007501:Iron / Q000494:pharmacology; D015227:Lipid Peroxidation / Q000187:drug effects*; D008786:Metmyoglobin / Q000502:physiology*
D006420:Hemeproteins; D008786:Metmyoglobin; D003300:Copper; D004492:Edetic Acid; D006861:Hydrogen Peroxide; D007501:Iron; D006735:Horseradish Peroxidase; D003676:Deferoxamine