A Copper Cage‐Complex as Mimic of the pMMO CuC Site. Issue 35 (19th July 2022)

• Record Type: Journal Article
• Authors: Bete, Sarah C.; May, Leander K.; Woite, Philipp; Roemelt, Michael; Otte, Matthias
• Is Part Of: Angewandte Chemie international edition. Volume 61:Issue 35(2022)
• Page Start: n/a
• Page End: n/a
• Publication Date: 2022-07-19
• Subjects: Biomimetic Synthesis -- Cage Compounds -- Enzyme Models -- Oxidation; Chemistry -- Periodicals; 540
• DOI: 10.1002/anie.202206120
• Languages: English
• ISSNs: 1433-7851

Abstract

Abstract: The active site of particulate methane monooxygenase (pMMO) and its mechanism of action are not known. Recently, the CuC site emerged as a potential active site, but to date it lacks any study on biomimetic resemblance of the coordination environment provided by the enzyme. Here, the synthesis of a cage ligand providing such an environment is reported. Copper is incorporated, and coordination occurs by the two imidazole and one carboxylate group offered by the ligand. Depending on the oxidation state, it can adopt different coordination modes, as evidenced by the solid‐state structures and computational investigation. The copper(I) state readily reacts with dioxygen and thereby undergoes CH activation. Moreover, the catalytic aerobic oxidation of hydroquinones as ubiquinol mimics is shown. Clean one‐electron oxidation occurs under mild conditions and EPR analysis of the copper(II) state in the presence of water reveals striking similarities to the data obtained from pMMO. Abstract : A series of copper complexes that replicate the CuC site of particulate methane monooxygenase is presented. Although this site is of great interest in the debate about the nature of the active site, it has not yet been modeled in a biomimetic study. The detailed replication leads to striking EPR similarities of the copper(II) state to purified pMMO. Further aerobic oxidation of hydroquinones as bioinspired substrates is shown.