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• W2046963859 abstract "The reaction between ferrimyoglobin, FeMb+(H2O), and hydrogen peroxide results in a one-equivalent oxidation of the hemoprotein giving a higher oxidation state of the molecule whose structure is best represented as a complex ferryl ion, FeMbO. A kinetic study of the formation of this compound, ferrylmyoglobin, shows that there are two reaction paths, the acidic form of ferrimyoglobin, FeMb+(H2O), reacting with H2O2, and either the alkaline form, FeMbOH, reacting with H2O2, or the acidic form reacting with O2H−. Two possible reaction mechanisms for the formation of ferrylmyoglobin are examined in the light of the quantitative kinetic data obtained. The first involves the production of an OH radical in a reaction similar to that usually written for the ferrous ion reaction, except that the oxidation states are all higher by 1 in the ferrimyoglobin reaction. The second involves the initial formation of a +5 oxidation state in the rate-determining step, which then undergoes extremely rapid reduction to ferrylmyoglobin by reducing groups present in the system (i.e., in the protein part of the molecule). In the latter mechanism, ferrimyoglobin would conform to the same pattern of oxidation-reduction behavior shown by the hemoprotein enzymes, peroxidase and catalase." @default.
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• W2046963859 date "1956-08-01" @default.
• W2046963859 modified "2023-09-25" @default.
• W2046963859 title "A kinetic study of the reaction between ferrimyoglobin and hydrogen peroxide" @default.
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• W2046963859 doi "https://doi.org/10.1016/0095-8522(56)90151-9" @default.
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