Abstract
The effects of low frequency magnetic field (0–12 mT) on hydrogen peroxide oxidized myoglobin-isolate (MbI) were investigated. The results indicate that the primary target of the hydrogen peroxide oxidation was Met(FeIII)Mb, leading to the fall off of iron ions from the porphyrin ring. Additionally, the increased magnetic field (≥9 mT) enhanced the release of more iron ions to react with H2O2, giving rise to the production of more hydroxyl radicals and the shift of oxidation site from porphyrin ring to Mb skeleton. Moreover, the directional movement of iron ions induced by magnetic field caused the generation of local micro-electric field and the rearrangement of charged groups on the protein surface or near-surface, thus affecting Mb aggregation. Overall, the magnetic field interfered with the hydrogen peroxide chain reaction process, changed the redox equivalents of Mb, and shifted the oxidation sites of Mb.
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