title: Copper-dioxygen complex mediated C-H bond oxygenation: relevance for particulate methane monooxygenase (pMMO).
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.
authors.affiliation: Department of Chemistry, The Johns Hopkins University, Baltimore, MD 21218, United States. rhimes1@jhu.edu
authors.forename: Richard A
authors.initials: RA
authors.lastname: Himes
authors.forename: Kenneth D
authors.initials: KD
authors.lastname: Karlin
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D020134:Catalytic Domain; D003300:Copper / Q000737:chemistry / Q000378:metabolism*; D018360:Crystallography, X-Ray; D008697:Methane / Q000378:metabolism; D010084:Oxidation-Reduction; D010100:Oxygen / Q000737:chemistry / Q000378:metabolism*; D010105:Oxygenases / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D001426:Bacterial Proteins; D003300:Copper; D010105:Oxygenases; C021555:methane monooxygenase; D008697:Methane; D010100:Oxygen