Alkane functionalization at nonheme iron centers. Mechanistic insights

Randolph A. Leising, Larry Que

Research output: Contribution to journalConference articlepeer-review

1 Scopus citations


Biological catalysts capable of functionalizing alkanes include cytochrome P450 (which contains a heme active site) and methane monooxygenase (MMO, which has a nonheme diiron active site). For cytochrome P450, an oxoiron (IV)(porphyrin cation radical) complex derived from the heterolysis of the O-O bond in an intermediate ferric peroxide is strongly implicated as the active species in the cytochrome P-450 mechanism. Little mechanistic insight into the nature of the oxidizing species has been obtained from these investigations. The authors intiated an investigation of the reactivity of iron complexes with tripodal ligands in combination with t-butyl hydroperoxide to gain insight into how nonheme iron centers may effect such chemistry. The tripodal ligands selected for this study offer the important advantage of systematic control over the ligand environment at a labile iron center.

Original languageEnglish (US)
Pages (from-to)318-323
Number of pages6
JournalAmerican Chemical Society, Division of Petroleum Chemistry, Preprints
Issue number1
StatePublished - Feb 1 1992
EventSymposium on Natural Gas Upgrading II - San Francisco, CA, USA
Duration: Apr 5 1992Apr 10 1992


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