† Department of Chemistry, Stanford University, Stanford, California 94305, United States
‡ Department of Chemistry and Biochemistry, California State University, Chico, California 95929, United States
J. Am. Chem. Soc., Article ASAP
DOI: 10.1021/jacs.5b02157
Publication Date (Web): May 28, 2015
Copyright © 2015 American Chemical Society
http://pubs.acs.org/doi/abs/10.1021/jacs.5b02157
† Department of Chemistry, Stanford University, Stanford, California 94305, United States
‡ Department of Chemistry and Biochemistry, California State University, Chico, California 95929, United States
http://pubs.acs.org/doi/abs/10.1021/jacs.5b02157
Abstract
The mechanisms of dioxygen activation and methane C−H oxidation in particulate methane monooxygenase (pMMO) are currently unknown. Recent studies support a binuclear copper site as the catalytic center. We report the low-temperature assembly of a high-valent dicopper(III) bis(μ-oxide) complex bearing marked structural fidelity to the proposed active site of pMMO. This unprecedented dioxygen-bonded Cu(III) species with exclusive biological ligation directly informs on the chemical plausibility and thermodynamic stability of the bis(μ-oxide) structure in such dicopper sites and foretells unusual optical signatures of an oxygenation product in pMMO. Though the ultimate pMMO active oxidant is still debated, C–H oxidation of exogenous substrates is observed with the reported Cu(III) complexes. The assembly of a high valent species both narrows the search for relevant pMMO intermediates and provides evidence to substantiate the role of Cu(III) in biological redox processes.
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