As seen in variant 1, the substrate was captivated by F263 (Phe 263) via a strong π-π interaction, and therefore a mutation of Phe to Leu in variant 2 removes the π-π interaction and allows the substrate to change its orientation. At the same instant, the substrate finds a new π-π interaction with the aromatic ring of tosyl moiety of iron nitrenoid. Due to the new π-π interaction, the substrate snuggles close to the tosyl moiety of the oxidant for the entire simulation. Therefore, the F263L mutation exerts a binding advantage that contributes to the enhanced activity. How do the mutations of A78V and A82L augment the enantioselectivity of the reaction?