Alternatives to the oxoferryl porphyrin cation radical as the proposed reactive intermediate of cytochrome P450: two-electron oxidized Fe(III) porphyrin derivatives

作者：Watanabe Y^*

来源：Journal of Biological Inorganic Chemistry, 2001, 6(8): 846-856.

DOI：10.1007/s007750100278

• heme enzyme
• cytochrome p450
• mechanism
• compound I

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.

• 出版日期2001-10