Models of oxidized heme proteins. Preparation and characterization of a trans-dioxoruthe nium(VI) porphyrin complex

John T. Groves, Robert Quinn

Research output: Contribution to journalArticle

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Abstract

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.

Original languageEnglish (US)
Pages (from-to)3844-3846
Number of pages3
JournalInorganic Chemistry
Volume23
Issue number24
DOIs
StatePublished - Mar 1984
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Physical and Theoretical Chemistry
  • Inorganic Chemistry

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