Syntheses and catalytic activities of new cytochrome P-450 model compounds. Effect of peptide chains

Article abstract of DOI:10.1246/bcsj.67.742

As cytochrome P-450 model compounds with structures similar to heme proteins, we designed and synthesized novel porphyrin iron (III) chloride complexes, 11 and 12, which have three peptide chains (3PCs) and four peptide chains (4PCs), and evaluated their catalytic activities. The asymmetric porphyrin complexes are derived from etioporphyrin and peptide chains equivalent to proteins were provided by ring-opening polymerization of N-carboxy L-amino acid anhydride (L-Phe-NCA, γ-BLG-NCA, and N(ε)-benzyloxycarbonyl-L-Lys-NCA) initiated by amino groups on meso positions. The new asymmetric porphyrin complex, 11 or 12, was used for asymmetric epoxidations of styrene as is done by cytochrome P-450. The iron complex achieved the induction of asymmetry, although it has no special conformation, and gave S-styrene oxide in excess (ca. 60%ee). It was found, furthermore, that asymmetric induction was affected by the kind of amino acid residue, the number of peptide chains, and length of peptide chains.