Reactions of Dioxygen and Its Reduced Forms with Heme Proteins and Model Porphyrin Complexes

Traylor, Teddy G.; Traylor, Patricia S.

doi:10.1007/978-1-4613-9783-0_3

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High-valent Iron(iv)-oxo Complexes Nam1

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2007

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“…This mechanism is similar to the O 2 activation by iron(II) porphyrins 58 and relevant to the catalytic cycle of methane monooxygenases (MMOs). 59 In the latter reaction, a dinuclear non-heme iron(II) complex activates O 2 to form a di(µ-oxo)diiron (IV) the capability of oxidizing the C-H bonds of cyclohexane at room temperature.…”

Section: High-valent Iron(iv)-oxo Complexes Nammentioning

confidence: 74%

High-Valent Iron(IV)–Oxo Complexes of Heme and Non-Heme Ligands in Oxygenation Reactions

2007

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High-valent iron(IV)-oxo species have been implicated as the key reactive intermediates in the catalytic cycles of dioxygen activation by heme and non-heme iron enzymes. Our understanding of the enzymatic reactions has improved greatly via investigation of spectroscopic and chemical properties of heme and non-heme iron(IV)-oxo complexes. In this Account, reactivities of synthetic iron(IV)-oxo porphyrin π-cation radicals and mononuclear nonheme iron(IV)-oxo complexes in oxygenation reactions have been discussed as chemical models of cytochrome P450 and non-heme iron enzymes. These results demonstrate how mechanistic developments in biomimetic research can help our understanding of dioxygen activation and oxygen atom transfer reactions in nature.

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Section: High-valent Iron(iv)-oxo Complexes Nammentioning

confidence: 74%