Abstract
Upon reactions with oxidants, hemoproteins retain their oxidizing equivalents not only in the heme iron, but also in the porphyrin or amino acid residues. HRP has a protein structure that stabilizes the porphyrin π-cation radical, which can easily be formed through various reactions. CCP reacts with H 2O 2 to form free radicals in amino acid residues as a catalytic intermediate species, which is stable in the absence of added electron donor. Ferric myoglobin apparently behaves as CCP, but its amino acid free radicals are unstable. These properties seem to be reflected on photooxidation of these hemoproteins.
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Schedule a callMore From: International Journal of Radiation Applications & Instrumentation. Part C, Radiation Physics & Chemistry
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