Journal
EUROPEAN JOURNAL OF INORGANIC CHEMISTRY
Volume -, Issue -, Pages -Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/ejic.202300516
Keywords
C-H activation; alcohol oxidation; copper; galactose oxidase mimic; photoredox catalysis
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This study investigates the mechanism of alcohol oxidation using a ferrocene-conjugated copper complex, offering valuable insights and potential for developing efficient and eco-friendly catalysts for chemical synthesis.
Enzyme mimic studies are driven by a variety of factors, including understanding the function of the active site, replicating enzyme activity, and constructing bio-inspired catalysts. In this study, we present a ferrocene-conjugated copper complex (FcTrpCOO)Cu(bpy) that not only serves as a structural analog of Galactose oxidase (GOase) but also demonstrates impressive catalytic efficiency for alcohol oxidation via a photoredox process. Mechanistic investigations of the reaction were carried out using a range of spectroscopic techniques, including UV-Vis, IR, CV, LC-MS, XAS, and EPR. These findings offer valuable insights into the mechanism of alcohol oxidation in biological systems and provide a promising approach for developing efficient and eco-friendly catalysts for chemical synthesis. The study introduces a dual catalysis method using photoredox and copper catalyst, enabling aldehyde formation. A newly designed ferrocene-conjugated copper complex, (FcTrpCOO)Cu(bpy), demonstrates effective catalytic alcohol oxidation via a photoredox mechanism. Mechanistic insights are gained through UV-Vis, IR, CV, LC-MS, XAS, and EPR spectroscopic techniques.+image
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