Manganese-dependent disproportionation of hydrogen peroxide in bicarbonate buffer.

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At physiological concentrations of HCO3- and CO2, Mn(II) catalyzes disproportionation of H2O2. This catalase-like activity is directly proportional to the concentrations of Mn(II) and H2O2, and it increases exponentially with increases in pH. The effect of increasing pH is almost completely attributable to the concomitant increase in HCO3- concentration. The rate is proportional to the third power of the HCO3- concentration, suggesting that 3 equivalents of HCO3- combine with 1 equivalent of Mn(II) to form the catalytic complex. It is presumed that the redox potential of the Mn(II) in equilibrium with Mn(III) couple in such a complex permits H2O2 to carry out facile reactions with Mn(II) comparable to those that occur with Fe(III) and Cu(II) chelate complexes, in which OH. and O2-. are established intermediates. The Mn-catalyzed disproportionation of H2O2 does not occur at physiological pH in the absence of HCO3-. Hepes, inorganic phosphate, and inorganic pyrophosphate inhibit the reaction catalyzed by the Mn/HCO3- system. These results are similar to those of Sychev et al. [Sychev, A.Y., Pfannmeller, U. & Isak, V.G. (1983) Russ. J. Phys. Chem. 57, 1690-1693]. The catalase-like activity of Mn(II)-bicarbonate complexes reported here, together with the superoxide dismutase activity of Mn complexes demonstrated by Archibald and Fridovich [Archibald, F.S. & Fridovich, I. (1982) Arch. Biochem. Biophys. 214, 452-463], strengthen the proposition that Mn may play an important role in the protection of cells against oxygen radical-mediated damage.

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