Mimicking the Cu<sub>D</sub> Site of pMMO via a Copper Cage‐Complex
The mechanism of action of particulate monooxygenase (pMMO) has yet to be determined. The Cu<sub>D</sub> 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.
Authors
- Michael Roemelt (ORCID: https://orcid.org/0000-0002-4780-5354)
- Matthias Otte (ORCID: https://orcid.org/0000-0001-6858-4960)
- Shu Miao (ORCID: https://orcid.org/0000-0002-5136-6569)
- Leon Gerndt
Institutions
- Humboldt-Universität zu Berlin (DE)
- Czech Academy of Sciences, Institute of Inorganic Chemistry (CZ)
- University of Göttingen (DE)
Publication Details
- Journal
- Chemistry - A European Journal
- Published
- 2025-03-12
- DOI
- https://doi.org/10.1002/chem.202500533
- Citations
- 1
- Primary Topic
- Metal-Catalyzed Oxygenation Mechanisms
- Type
- article
- Field-Weighted Citation Impact
- 0.54