Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 134, Issue 27, Pages 11112-11115Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja304357z
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Funding
- KRF/MEST of Korea through CRI
- KRF/MEST of Korea through GRL [2010-00353]
- KRF/MEST of Korea through WCU [R31-2008-000-10010-0]
- National Research Foundation of Korea [2010-00353, R31-2012-000-10010-0] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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Metal-superoxo species are believed to play key roles in oxygenation reactions by metalloenzymes. One example is cysteine dioxygenase (CDO) that catalyzes the oxidation of cysteine with O-2, and an iron(III)-superoxo species is proposed as an intermediate that effects the sulfoxidation reaction. We now report the first biomimetic example showing that a chromium(III)-superoxo complex bearing a macrocyclic TMC ligand, [Cr-III(O-2)(TMC)(Cl)](+), is an active oxidant in oxygen atom transfer (OAT) reactions, such as the oxidation of phosphine and sulfides. The electrophilic character of the Cr(III)-superoxo complex is demonstrated unambiguously in the sulfoxidation of para-substituted thioanisoles. A Cr(IV)-oxo complex, [Cr-IV(O)(TMC)(Cl)](+), formed in the OAT reactions by the chromium(III) superoxo complex, is characterized by X-ray crystallography and various spectroscopic methods. The present results support the proposed oxidant and mechanism in CDO, such as an iron(III) superoxo species is an active oxidant that attacks the sulfur atom of the cysteine ligand by the terminal oxygen atom of the superoxo group, followed by the formation of a sulfoxide and an iron(IV)-oxo species via an O-O bond cleavage.
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