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Abstract
The mechanism of action of particulate monooxygenase(pMMO) has yet to be determined. The CuDsite with two histidinesand an asparagine coordinating to copper has been identified as apotential active site of pMMO. Here, we present a copper cagecomplex, that assembles this coordination sphere, being a structuralmimic of the pMMO. The cage is capable to catalyze aerobicoxidations of organic substrates such as benzylic alcohols toaldehydes and hydroquinones to quinones. This is inspired by the reactivity that is observed for enzymatic active sites possessing copper.
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