Bioinspired Photoredox Oxidation of Alcohols with Copper‐Containing Galactose Oxidase Analog

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 structur...

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Veröffentlicht in:European journal of inorganic chemistry 2024-01, Vol.27 (3), p.n/a
Hauptverfasser: Chiang, Chien‐Wei, Chou, Yi‐Hsien, Chou, Chih‐Hui, Chen, Hung‐Chi, Chen, Jeng‐Lung, Hsu, Liang‐Ching, Huang, Wei‐Hsiang, Li, Hung‐Li, Liu, Yu‐Hao
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Sprache:eng
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Zusammenfassung: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.
ISSN:1434-1948
1099-0682
DOI:10.1002/ejic.202300516