Journal
ACCOUNTS OF CHEMICAL RESEARCH
Volume 40, Issue 7, Pages 522-531Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ar700027f
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Funding
- National Research Foundation of Korea [R16-2003-004-01001-0] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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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 remmove-cation radicals and mononuclear non-heme 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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