Figure 2. Steady-state Kinetic Parameters for (A) Mn (II) and (B) ABTS Oxidation by Wild-type and Mutant MnP3 Enzymes from Phlebia radiata.Each data point represents the mean of three independent determinations with standard errors indicated. Assays were carried out as described in materials and methods. For assays with Mn (II), a fixed concentration of 0.1 mM H2O2 was used and the data fitted to the Michaelis equation using Sigma Plot. For ABTS studies, a fixed concentration of 0.01 µM was used for all assays involving the wild-type enzyme while that of the mutant variants range from 0.1 – 6.5 mM. The kinetic parameters extracted from the plots are presented in Table 1 : Role of Some Metal Ions on Steady–state Kinetics of Engineered Wild–type and Manganese (II) Binding Site Mutants of Recombinant Phlebia radiata Manganese Peroxidase 3 (rPr-MnP3) : Science and Education Publishing

Figure 2. Steady-state Kinetic Parameters for (A) Mn (II) and (B) ABTS Oxidation by Wild-type and Mutant MnP3 Enzymes from Phlebia radiata.Each data point represents the mean of three independent determinations with standard errors indicated. Assays were carried out as described in materials and methods. For assays with Mn (II), a fixed concentration of 0.1 mM H₂O₂ was used and the data fitted to the Michaelis equation using Sigma Plot. For ABTS studies, a fixed concentration of 0.01 µM was used for all assays involving the wild-type enzyme while that of the mutant variants range from 0.1 – 6.5 mM. The kinetic parameters extracted from the plots are presented in Table 1

American Journal of Medical and Biological Research. 2016, 4(3), 42-52 doi:10.12691/ajmbr-4-3-2