pH-Dependence of Manganese (II) Oxidation Reaction by Novel Wild-Type and Mutants Recombinant <i>Phlebia radiata</i> Manganese Peroxidase 3 (rPr-MnP3) Enzymes — Oak Academic Publishing
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pH-Dependence of Manganese (II) Oxidation Reaction by Novel Wild-Type and Mutants Recombinant <i>Phlebia radiata</i> Manganese Peroxidase 3 (rPr-MnP3) Enzymes
Department of Genetics and Biotechnology, Faculty of Biological Sciences, Akwa Ibom State University, Uyo, Akwa Ibom State, Nigeria
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Department of Biochemistry, Faculty of Sciences, University of Uyo, Akwa Ibom State, Uyo, Akwa Ibom State, Nigeria
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Department of Chemical Engineering and Analytical Science, University of Manchester, Manchester, UK
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Department of Genetics and Biotechnology, Faculty of Biological Sciences, Akwa Ibom State University, Uyo, Akwa Ibom State, Nigeria
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Department of Genetics and Biotechnology, Faculty of Biological Sciences, Akwa Ibom State University, Uyo, Akwa Ibom State, Nigeria
1 Department of Genetics and Biotechnology, Faculty of Biological Sciences, Akwa Ibom State University, Uyo, Akwa Ibom State, Nigeria
2 Department of Biochemistry, Faculty of Sciences, University of Uyo, Akwa Ibom State, Uyo, Akwa Ibom State, Nigeria
3 Department of Chemical Engineering and Analytical Science, University of Manchester, Manchester, UK
4 Department of Genetics and Biotechnology, Faculty of Biological Sciences, Akwa Ibom State University, Uyo, Akwa Ibom State, Nigeria
5 Department of Genetics and Biotechnology, Faculty of Biological Sciences, Akwa Ibom State University, Uyo, Akwa Ibom State, Nigeria
The goal of this study was to determine whether mutation of the Mn-binding site of wild-type recombinant Phlebia radiata manganese peroxidase 3 affected the pH-dependence kinetic parameters. pH range investigated was 2.5 – 12.0. The catalytic efficiency of the mutant enzymes at high and low pH in comparison to the wild-type was investigated using standard rPr-MnP3 protocol. Wild-type recombinant Phlebia radiata MnP3 enzyme showed optimal activity with Mn (II) as substrate at pH 5.0 and remained moderately active (approximately 40%) in the pH range of 6.0 - 9.0. The rPr-MnP3 mutants’ maximum activity ranged between 5.5 and 8.0. Wild-type and mutants rPr-MnP3 enzymes exhibited a similar pH profile with optimum pH of 3.0 for ABTS oxidation. Mutation has severely decreased the catalytic efficiency for Mn (II) oxidation at pH 5.0. The rPr-MnP3 enzymes showed enhanced affinity for Mn (II) at alkaline pH and a more alkaline range for catalysis than ever reported for any Manganese Peroxidase. This study reveals that at higher pH, rPr-MnP3 can function with alternative ligands in the Mn (II) site and does not have an absolutely obligate requirement for an all carboxylate ligand set. These results further strongly confirm that Mn 2+ binding site is the only productive catalytic site for Mn (II) oxidation.
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