The Generation of Ferryl or Hydroxyl Radicals During Interaction of Hemeproteins with Hydrogen Peroxide

  • Joseph Kanner
  • Stella Harel
  • Avior Menahem Salan
Part of the Basic Life Sciences book series (BLSC, volume 49)

Abstract

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.

Keywords

Peroxide Hydroxyl EDTA Catalysis Superoxide 

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Copyright information

© Plenum Press, New York 1988

Authors and Affiliations

  • Joseph Kanner
    • 1
  • Stella Harel
    • 1
  • Avior Menahem Salan
    • 1
  1. 1.Department of ScienceVolcani CenterBet DaganIsrael

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