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Hemoglobin. A biologic fenton reagent.

S M Sadrzadeh, E Graf, S S Panter

    The Journal of Biological Chemistry
    |December 10, 1984
    PubMed
    Summary
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    Free hemoglobin can generate harmful hydroxyl radicals, similar to a Fenton reagent, particularly during inflammation. The protein haptoglobin effectively blocks this damaging process, suggesting a key protective role.

    Area of Science:

    • Biochemistry
    • Cellular Biology
    • Oxidative Stress Research

    Background:

    • Iron compounds are known to facilitate hydroxyl radical generation from reactive oxygen species.
    • Previous research focused on low-molecular-weight iron compounds, leaving the role of complex iron-rich substances like hemoglobin unexplored.

    Purpose of the Study:

    • To investigate whether free hemoglobin can mediate hydroxyl radical generation.
    • To explore the mechanism of hemoglobin-induced hydroxyl radical formation and its biological implications.

    Main Methods:

    • Utilized a superoxide anion-generating system (hypoxanthine and xanthine oxidase) to assess hemoglobin's effect.
    • Examined the impact of hemoglobin oxidation, carbon monoxide binding, and enzyme additions (catalase, superoxide dismutase) on radical generation.

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  • Assessed the peroxidation of poly-unsaturated fatty acids and red cell membrane lipids.
  • Investigated the effect of haptoglobin on hemoglobin-mediated reactions.

    • Main Results:

    • Hemoglobin dose-dependently promoted hydroxyl radical formation in the presence of superoxide.
    • Hydroxyl radical generation was significantly reduced by hemoglobin oxidation, carbon monoxide, and catalase, implicating ferrous heme iron and hydrogen peroxide (H2O2).
    • Hemoglobin enhanced lipid peroxidation, which was suppressed by haptoglobin.

    Conclusions:

    • Free hemoglobin acts as a Fenton-like reagent, catalyzing hydroxyl radical generation and potentially contributing to oxidative damage in inflammatory conditions.
    • Haptoglobin effectively inhibits hemoglobin-mediated hydroxyl radical and lipid peroxidation, suggesting a crucial physiological role in preventing such oxidative harm.