High-valent iron porphyrin complexes have been suggested for the oxidized states of the peroxidases, 1 and similar intermediates have been implicated in the oxygen-transfer reactions of cytochrome P-4502 and the dioxygen reduction of cytochrome oxidase.3 An understanding of the redox chemistry mediated by these enzymes has been hampered by the install bility of these oxidized iron-heme intermediates and by the lack of simple chemical models for these reactive states. Synthetic examples of an oxoiron(IV) prophryin4 and an oxoiron(IV) porphyrin cation radical5 are now known; however, the thermal instability of each has prevented their isolation as pure solids. The periodic relationship of iron and ruthenium suggests that the latter could provide stable examples of oxidized metalloporphyrins.
All Science Journal Classification (ASJC) codes
- Physical and Theoretical Chemistry
- Inorganic Chemistry