Abstract
The effects of replacement of the axial methionine 80 heme ligand with a non-coordinating alanine on the peroxidase activity of kaolinite-immobilized cytochrome c were investigated at different pH values. The catalytic activity of the adsorbed mutant was found to be remarkably higher than that of wild-type cytochrome c. The pH dependence of Vmax and KM values is discussed in terms of accessibility of the substrates to the metal center and surface charge of kaolinite. Our approach, based on the combined use of adsorption on kaolinite and protein engineering, endows this bioinorganic interface with remarkable catalytic properties.
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