A Ferromagnetically Coupled (S=1) Peroxodicopper(II) Complex1. (21st December 2014)

• Record Type: Journal Article
• Authors: Kindermann, Nicole; Bill, Eckhard; Dechert, Sebastian; Demeshko, Serhiy; Reijerse, Edward J.; Meyer, Franc
• Is Part Of: Angewandte Chemie. Volume 127:Number 6(2015)
• Page Start: 1758
• Page End: 1763
• Publication Date: 2014-12-21
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1002/ange.201409709
• Languages: English
• ISSNs: 0044-8249

Abstract

<abstract abstract-type="main" xml:lang="en"> <title>Abstract</title> <p>Copper enzymes play important roles in the binding and activation of dioxygen in biological systems. Key copper/dioxygen intermediates have been identified and studied in synthetic analogues of the metalloprotein active sites, including the μ‐η²:η²‐peroxodicopper(II) motif relevant to type III dicopper proteins. Herein, we report the synthesis and characterization of a bioinspired dicopper system that forms a stable μ‐η¹:η¹‐peroxo complex whose Cu‐O‐O‐Cu torsion is constrained to around 90° by ligand design. This results in sizeable ferromagnetic coupling between the copper(II) ions, which is detected by magnetic measurements and HF‐EPR spectroscopy. The new dicopper peroxo system is the first with a triplet ground state, and it represents a snapshot of the initial stages of O₂ binding at type III dicopper sites.</p> </abstract>