ABSTRACTQuantitative analysis of the interactions of ·OH and eāq̄with ferri‐myoglobin in neutral aqueous solution provides a basis for evaluating earlier studies of the radiolysis of myoglobin. γ‐radiolysis of deaerated solutions in which either ·OH or eāq̄predominates leads to the formation of both deoxymyoglobin and ferrimyoglobin peroxide. Correction for a post‐irradiation thermal process allows radiation‐induced composition changes to be separately investigated. Depending on the radical system under consideration, a specific steady‐state composition is reached at moderate doses that involves the ferri, deoxy, and ferri‐peroxide forms of the myoglobin. Aeration of irradiated solutions quantitatively converts the deoxymyoglobin to oxymyoglobin. Radiolysis of oxygenated solutions containing N2O generates only ferrimyoglobin peroxide. Earlier studies on the radiolysis of ferrimyoglobin have been reevaluated in light of novel features that have emerged in
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