Alkane Oxidation: Methane Monooxygenases, Related Enzymes, and Their Biomimetics
Publication in refereed journal

香港中文大學研究人員
替代計量分析
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其它資訊
摘要Methane monooxygenases (MMOs) mediate the facile conversion of methane into methanol in methanotrophic bacteria with high efficiency under ambient conditions. Because the selective oxidation of methane is extremely challenging, there is considerable interest in understanding how these enzymes carry out this difficult chemistry. The impetus of these efforts is to learn from the microbes to develop a biomimetic catalyst to accomplish the same chemical transformation. Here, we review the progress made over the past two to three decades toward delineating the structures and functions of the catalytic sites in two MMOs: soluble methane monooxygenase (sMMO) and particulate methane monooxygenase (pMMO). sMMO is a water-soluble three-component protein complex consisting of a hydroxylase with a nonheme diiron catalytic site; pMMO is a membrane-bound metalloenzyme with a unique tricopper cluster as the site of hydroxylation. The metal cluster in each of these MMOs harnesses O2 to functionalize the CH bond using different chemistry. We highlight some of the common basic principles that they share. Finally, the development of functional models of the catalytic sites of MMOs is described. These efforts have culminated in the first successful biomimetic catalyst capable of efficient methane oxidation without overoxidation at room temperature.
著者Vincent C.-C. Wang, Suman Maji, Peter P.-Y. Chen, Hung Kay Lee, Steve S.-F. Yu, Sunney I. Chan
期刊名稱Chemical Reviews
出版年份2017
卷號117
期次13
出版社American Chemical Society
出版地USA
頁次8574 - 8621
國際標準期刊號0009-2665
電子國際標準期刊號1520-6890
語言美式英語
關鍵詞Alkane oxidation, methane monooxygenases, copper complexes, biomimetic models

上次更新時間 2021-15-01 於 01:07