Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 54, Issue 6, Pages 1738-1743Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201409709
Keywords
bioinorganic chemistry; copper; EPR spectroscopy; magnetic properties; peroxo complexes
Categories
Funding
- Fonds der Chemischen Industrie
- Studienstiftung des deutschen Volkes
- DFG [IRTG 1422]
Ask authors/readers for more resources
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 -(2):(2)-peroxodicopper(II) motif relevant to typeIII dicopper proteins. Herein, we report the synthesis and characterization of a bioinspired dicopper system that forms a stable -(1):(1)-peroxo complex whose Cu-O-O-Cu torsion is constrained to around 90 degrees 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 O-2 binding at typeIII dicopper sites.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available