Alternatives to the oxoferryl porphyrin cation radical as the proposed reactive intermediate of cytochrome P450: two-electron oxidized Fe(III) porphyrin derivatives.
The active intermediates in most heme enzyme-catalyzed oxidations such as epoxidation and hydroxylation have been attributed to the O=Fe(IV) porphyrin pi-cation radical, so-called compound I. This could be correct for many cases, however, alternatives to compound I have been proposed for several oxidations including aliphatic hydroxylation catalyzed by P450. Therefore, two-electron oxidized iron porphyrin complexes other than compound I have been reviewed as candidates for the active species responsible for oxidations catalyzed by heme enzymes.
Watanabe
Y
Y
Institute for Molecular Science, Okazaki 444-8585, Japan. yoschi@ims.ac.jp
D000475:Alkenes / Q000737:chemistry; D001141:Aromatase / Q000737:chemistry; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry*; D005290:Ferric Compounds / Q000737:chemistry*; D006860:Hydrogen Bonding; D008665:Metalloporphyrins / Q000737:chemistry*; D019001:Nitric Oxide Synthase / Q000737:chemistry; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000737:chemistry; D058886:Sterol 14-Demethylase
D000475:Alkenes; D005290:Ferric Compounds; D008665:Metalloporphyrins; D003577:Cytochrome P-450 Enzyme System; D010088:Oxidoreductases; D019001:Nitric Oxide Synthase; D001141:Aromatase; D058886:Sterol 14-Demethylase