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• W2023919891 abstract "P-Hydroquinone and catechol catalytically promote the oxidation of oxyhemoglobin and Oxymyoglobin to the ferriform. Kinetic data for oxyhemoglobin oxidation indicates a first-order dependence upon the hemeprotein concentration and half-order dependence upon diphenol; however at high catalyst concentration, saturation is observed with similar V values for both diphenols despite the difference in reactivity. It is proposed that initially formed quinone oxidizes the hemeprotein with oxygen release; in turn, the semiquinone oxidizes a second molecule of hemeprotein and regenerates the quinone, with the bound oxygen acquiring two electrons. Except for the more reactive oxymyoglobin, the reduced form of the catalyst must be present to oppose semiquinone disappearance by dismutation. Since the expected release of O2 for water formation is observed, the system may be considered a model for terminal oxidase, the couple QS replacing a Fe2+Fe2+ or a Cu+Cu2+ system. It is tentatively inferred that oxyhemoglobin has the structure HbFe2+---O2 and that the rate of the catalyzed oxidation is limited by the rate of generation of the true reacting form, the superoxide ferri structure, HbFe3+---O2−." @default.
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• W2023919891 date "1975-06-01" @default.
• W2023919891 modified "2023-10-16" @default.
• W2023919891 title "The effect of diphenols upon the autoxidation of oxyhemoglobin and oxymyoglobin" @default.
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• W2023919891 doi "https://doi.org/10.1016/0003-9861(75)90286-6" @default.
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