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  • Title: Peroxidase activity of the hemeoctapeptide N-acetylmicroperoxidase-8.
    Author: Marques HM.
    Journal: Inorg Chem; 2005 Sep 05; 44(18):6146-8. PubMed ID: 16124790.
    Abstract:
    The pH dependence of the peroxidase activity (guaiacol assay) of the ferric hemeoctapeptide N-acetylmicroperoxidase-8 (N-AcMP8) was studied under conditions where formation of the Compound I analogue of the peroxidase enzymes is rate limiting. The pH profile of the reaction rate is consistent with a mechanism where both H2O2 and HO2- can displace H2O coordinated trans to neutral His but where the hydroxo complex of the hemepeptide (OH- trans to His) is kinetically inert. At pH > 11, where the proximal His ligand of Fe(III) ionizes to form a histidinate, the hydroxo complex (OH- trans to His-) becomes kinetically labile. A comparison of DeltaH(double dagger) and DeltaS(double dagger) values for the reaction of H2O2 and HO2-, obtained from the temperature dependence of the rate constants, with values for CN- and cysteine reported previously, shows that the activation parameters depend on the identity of the incoming ligand. This suggests that ligand substitution at Fe(III) in N-AcMP8 proceeds through an interchange mechanism.
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