Desferrioxamine as an Electron Donor. Inhibition of Membranal Lipid Peroxidation Initiated by H202–Activated Metmyoglobin and Other Peroxidizing Systems
- 1 January 1987
- journal article
- research article
- Published by Taylor & Francis in Free Radical Research Communications
- Vol. 3 (1-5) , 309-317
- https://doi.org/10.3109/10715768709069798
Abstract
Desferoxamine (DFO) involvement in several peroxidative systems was studied. These sytems included: a) membranal lipid peroxidation initiated by H2O2-activated metmyoglobin (or methemoglobin); b) phenol-red oxidation by activated metmyoglobin or horseradish peroxidase (HRP): c) β-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 H202-horseradish peroxidase was inhibited competitively with DFO. Kinetic studies using the spectra changes in the Soret region of metmyoglobin suggest a mechanism by which H202 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.Keywords
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