Effect of single-site charge-reversal mutations on the catalytic properties of yeast cytochrome c peroxidase: Mutations near the high-affinity cytochrome c binding site

Fifteen single-site charge-reversal mutations of yeast cytochrome c peroxidase (CcP) are constructed to examine the effect of localized charge on the catalytic properties of the enzyme. The results have shown that five of the 15 mutations cause large increases in the Michaelis constant, thus indicating that the cytochrome c-CcP complex is the dominant catalytically active complex in solution.