Mimicking the CuD Site of pMMO via a Copper Cage‐Complex

The mechanism of action of particulate monooxygenase (pMMO) has yet to be determined. The CuD site with two histidines and an asparagine coordinating to copper has been identified as a potential active site of pMMO. Here, we present a copper cage complex, that assembles this coordination sphere, being a structural mimic of the pMMO. The cage is capable to catalyze aerobic oxidations of organic substrates such as benzylic alcohols to aldehydes and hydroquinones to quinones. This is inspired by the reactivity that is observed for enzymatic active sites possessing copper.