Copper-dioxygen complex mediated C-H bond oxygenation: relevance for particulate methane monooxygenase (pMMO).
Copper-dioxygen complex mediated C-H bond oxygenation: relevance for particulate methane monooxygenase (pMMO).
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DOI：
10.1016/j.cbpa.2009.02.025
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发表时间：
2009-02
影响因子：
7.8
通讯作者：
Karlin, Kenneth D.
中科院分区：
文献类型：
--
作者：
Himes, Richard A.;Karlin, Kenneth D.
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-O2 chemistry that may contribute to an understanding of copper-ion mediated hydrocarbon oxidation chemistry.
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