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. Author manuscript; available in PMC: 2012 Sep 1.
Published in final edited form as: Free Radic Biol Med. 2010 Oct 27;51(5):1062–1067. doi: 10.1016/j.freeradbiomed.2010.10.704

Figure 1. Mechanism for Mb-induced lipid peroxidation and its inhibition by acetaminophen.

Figure 1

Oxidation of ferric Mb (Fe(III)Mb) by a lipid hydroperoxide (LOOH) yields the ferryl Mb protoporphyrin radical (Fe(IV)=O PPIX •). This radical can delocalize to the protein to form a globin radical (Mb •), which can in turn catalyze lipid peroxidation by abstracting an electron from a lipid (LH). The lipid radical (L •) can then react to molecular oxygen to form the peroxyl radical (LOO •), which can propagate lipid peroxidation. Reducing co-substrates such as ApAP (RH) reduce the ferryl Mb back to its ferric state, thus inhibiting Mb-catalyzed lipid peroxidation.