title: A ferromagnetically coupled (S = 1) peroxodicopper(II) complex.
abstract: 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-η(2):η(2)-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-η(1):η(1)-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.
authors.affiliation: Institut für Anorganische Chemie, Georg-August-Universität Göttingen, Tammannstrasse 4, 37077 Göttingen (Germany) http://www.meyer.chemie.uni-goettingen.de.
authors.forename: Nicole
authors.initials: N
authors.lastname: Kindermann
authors.forename: Eckhard
authors.initials: E
authors.lastname: Bill
authors.forename: Sebastian
authors.initials: S
authors.lastname: Dechert
authors.forename: Serhiy
authors.initials: S
authors.lastname: Demeshko
authors.forename: Edward J
authors.initials: EJ
authors.lastname: Reijerse
authors.forename: Franc
authors.initials: F
authors.lastname: Meyer
mesh_terms: D003300:Copper / Q000737:chemistry*; D004578:Electron Spin Resonance Spectroscopy; D007501:Iron / Q000737:chemistry*; D008280:Magnetics; D008958:Models, Molecular; D013059:Spectrum Analysis, Raman
chemical_list: D003300:Copper; D007501:Iron
keywords: EPR spectroscopy; bioinorganic chemistry; copper; magnetic properties; peroxo complexes