Modulation of redox potential and alteration in reactivity via the peroxide shunt pathway by mutation of cytochrome P450 around the proximal heme ligand

Single site-directed mutants F310A and A320Q and double mutant F310A/A320Q are constructed and all mutant enzymes as well as wild-type (WT) cytochrome P450 from the thermoacidophilic crenarchaeon Sulfolobus tokodaii strain 7 (P450st) are expressed at high levels. The results have shown that the reduction potential and electron density on the heme iron are modulated by the Phe310 and Ala320 residues in P450st.