The Generation of Ferryl or Hydroxyl Radicals During Interaction of Hemeproteins with Hydrogen Peroxide
Previous evidence for hydroxyl radical generation in ferric ion-derived Fenton reactions was presented by Walling et al.1 and Gutteridge2. Methemoglobin (MetHb) and metmyoglobin (MetMb), the ferric states of these proteins, are activated by H2O2 producing a short-lived intermediate composed of one oxidizing equivalent on the heme, forming a ferryl, and one on the globin, i.e. giving an oxo-ferryl hemeglobin radical3. Studies on metmyoglobin-peroxide show that although it is not identical with compounds I or II or horseradish peroxidase (HRP), it has some structural features in common with both4.
KeywordsFenton Reaction Free Iron Hydroxyl Radical Scavenger Membranal Lipid Peroxidation Hydroxyl Radical Formation
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