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Curr Opin Chem Biol. 2009 Feb;13(1):119-31. doi: 10.1016/j.cbpa.2009.02.025. Epub 2009 Mar 13.

Copper-dioxygen complex mediated C-H bond oxygenation: relevance for particulate methane monooxygenase (pMMO).

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  • 1Department of Chemistry, The Johns Hopkins University, Baltimore, MD 21218, United States. rhimes1@jhu.edu

Abstract

Particulate methane monooxygenase (pMMO), an integral membrane protein found in methanotrophic bacteria, catalyzes the oxidation of methane to methanol. Expression and greater activity of the enzyme in the presence of copper ion suggest that pMMO is a cuprous metalloenzyme. Recent advances - especially the first crystal structures of pMMO - have energized the field, but the nature of the active site(s) and the mechanism of methane oxidation remain poorly understood-yet hotly contested. Herein the authors briefly review the current understanding of the pMMO metal sites and discuss advances in small molecule Cu-O(2) chemistry that may contribute to an understanding of copper-ion mediated hydrocarbon oxidation chemistry.

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PMID:
19286415
[PubMed - indexed for MEDLINE]
PMCID:
PMC2676220
Free PMC Article
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