In summary, oxidative stable VP mutants were successfully
obtained by rational protein engineering. Oxidizable residues and
those close to H2O2-binding pocket and heme exerted great influence
on H2O2 stability of VP, some mutants displayed dramatically
increased H2O2 tolerance and/or catalytic efficiencies. These strategies
would be applicable for improving H2O2 resistance of other
heme proteins, and the present results will be useful for potential
industrial use of VP and further engineering VP toward higher
oxidative stability and catalytic efficiency