Mechanistic Insight into Alcohol Oxidation by High-Valent Iron-Oxo Complexes of Heme and Nonheme LigandsThis research was supported by the Ministry of Science and Technology of Korea through Creative Research Initiative Program.
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چکیده
High-valent iron–oxo species are frequently invoked as the key intermediates in the catalytic oxidation of organic substrates by heme and nonheme iron mono-oxygenases. In the case of heme-containing enzymes such as cytochromes P450, oxoiron(iv) porphyrin p-cation radicals have been proposed as active oxidants that effect a number of oxidation reactions, which include alkane hydroxylation, olefin epoxidation, and alcohol oxidation. Indeed, a number of synthetic oxoiron(iv) porphyrin p-cation radicals have been prepared and used in mechanistic studies of alkane hydroxylation and olefin epoxidation. In mononuclear nonheme iron enzymes, oxoiron(iv) intermediates have been unveiled very recently in enzymatic and biomimetic reactions. The mononuclear nonheme oxoiron(iv) species have been well-characterized with various spectroscopic techniques and with X-ray crystallography and were shown to be active in a variety of oxidation reactions such as alkane hydroxylation, olefin epoxidation, and the oxidation of sulfides and PPh3. [4–6] The oxidation of alcohols to the corresponding carbonyl compounds is an important chemical process in industrial and
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