Mimicking the CuD Site of pMMO via a Copper Cage‐Complex
Year: 2025
Type: article
Abstract: 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.
Source: Chemistry - A European Journal
Authors: Shunyi Miao, Leon Gerndt, Michael Roemelt, Matthias Otte
Institutions: University of Göttingen, Humboldt-Universität zu Berlin
Language: English
Subfield: Inorganic Chemistry
Field: Chemistry
Domain: Physical Sciences
Open Access status: hybrid
Estimated APC paid: $4,640
Funder: Deutsche Forschungsgemeinschaft
OpenAlex ID: W4408260034
