Abstract
Publisher Summary This chapter discusses the peroxidative activities of hemoglobin and hemoglobin derivatives. Methemoglobin and metmyoglobin can react with preexisting lipid hydroperoxides to yield lipid-associated free radicals, which resulted in the propagation of free radical-mediated reactions that produced extensive lipid peroxidation. Methemoglobin and metmyoglobin can initiate the peroxidation of polyunsaturated fatty acids. Substantial membrane lipid peroxidation for model cells composed of hemoglobin entrapped in chemically defined liposomes. Human erythrocytes are also shown to be susceptible to hemoglobin-catalyzed, H 2 O 2 -dependent lipid peroxidation. Additionally, lipids, proteins, and carbohydrates are also susceptible to oxidative degradation by hemoglobin. Thus, the addition of H 2 O 2 to erythrocytes or erythrocyte membranes produces high molecular weight membrane protein aggregates, whereas deoxyribose is readily degraded by H 2 O 2 in the presence of hemoglobin. The mechanism by which hemoglobin exerts its peroxidative activity is similar to that of the peroxidases, in which hydrogen peroxide first reacts with the native enzyme and withdraws two electrons.
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