Institut für Anorganische Chemie, Georg-August-Universität Göttingen, Tammannstrasse 4, 37077 Göttingen (Germany) http://www.meyer.chemie.uni-goettingen.de.
Angew Chem Int Ed Engl. 2015 Feb 2;54(6):1738-43. doi: 10.1002/anie.201409709. Epub 2014 Dec 21.
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.
铜酶在生物系统中氧的结合和活化中起着重要作用。在金属蛋白活性位点的合成类似物中，已经确定并研究了关键的铜/氧中间体，包括与 III 型双铜蛋白相关的μ-η(2):η(2)-过氧二铜(II)基序。在此，我们报告了一种生物启发的双铜系统的合成与表征，该系统形成了一个稳定的μ-η(1):η(1)-过氧配合物，其 Cu-O-O-Cu 扭转通过配体设计被限制在约 90°。这导致铜(II)离子之间存在可观的铁磁耦合，这可以通过磁测量和 HF-EPR 光谱检测到。新的双铜过氧系统是第一个具有三重态基态的系统，它代表了 III 型双铜位点上 O2 结合初始阶段的一个快照。
