Journal
CURRENT OPINION IN CHEMICAL BIOLOGY
Volume 13, Issue 1, Pages 119-131Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/j.cbpa.2009.02.025
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Funding
- National Institutes of Health [GM 28962]
- RAH [1732 AG026923]
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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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