[Effect of pH on the oxidase activity of ceruloplasmin].

The effect of pH on the kinetic parameters (Kms, Vs) of the reaction of adrenaline and Fe(II) (More's salt) oxidation by ceruloplasmin isolated from human donor blood was investigated. It was assumed that the imidazole group of histidine is functionally important for the above reactions. For Fe(II) the effect of the ionizeable group was observed during substrate binding to the ceruloplasmin molecule, whereas in the course of the adrenaline oxidation reaction it manifests itself during catalytic interaction of the substrate with the enzyme. The organic substrate can bind both to the protonated and to the non-protonated form of the enzyme. Fe(II) interacts only with the protonated form of the protein. In both cases, the rate-limiting step of the oxidase reaction is preceded by a single step, i.e., proton binding. The schemes describing the order of proton attachment in the course of the above reactions are proposed.