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  • Title: Study of ceruloplasmin oxidase activity. The effect of pH.
    Author: Saenko EL, Siverina OB, Basevich VV, Yaropolov AI.
    Journal: Biochem Int; 1990; 20(6):1049-58. PubMed ID: 2369410.
    Abstract:
    To find out the mechanism of ceruloplasmin (CP) oxidase activity CP interaction with organic substrates adrenaline (AD), catechol, p-phenylenediamine) and Fe2+ was investigated. CP was shown to interact with the above substrates according to the Theorell-Chance mechanism to form a kinetically insignificant ternary complex. The oxygen molecule binds first to CP followed by the molecule of electron donor: the inhibition of enzymatic oxidation by the reaction product is competitive. The effects of pH on kinetic parameters (Ksm, Vs) of oxidation reactions of AD and Fe2+ in the presence of CP were examined. AD was shown to be able to bind both to the protonated and to the non-protonated form of CP whereas Fe2+ interacts only with the protonated form: the rate of catalytic event (Vs) is influenced by pH in the presence of AD whereas in the presence of Fe2+ only binding to CP (Ksm) is affected by pH. Kinetic schemes describing the order of binding of hydrogen ions in the course of above reactions are proposed.
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