INOR 937 |
| The recent structural characterization of the active site of the enzyme nitrous oxide reductase (N2OR) revealed an unusual configuration in which four copper centers are bridged by a single inorganic sulfide ion. As both the reduction of nitrous oxide at a copper center and the tetracopper-sulfide coordination are unprecedented in Nature, recent efforts have focused on understanding the mechanism of the reaction and the role of the sulfur ion in the catalytic pathway. While synthetic model complexes should provide a more fundamental understanding of copper-sulfur interactions that are relevant to N2OR, examples having biologically relevant N-donor ligands are rare. We present here a variety of novel copper-sulfide clusters synthesized by the addition of sulfur reagents to mononuclear copper(I) and copper(II) complexes bearing simple amine ligands. These complexes demonstrate interesting structural, electronic, and spectroscopic characteristics which provide insight into the nature of copper-sulfur bonding interactions and possible roles of the sulfide ion in nitrous oxide reductase. |
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Bioinorganic Modeling
1:30 PM-5:30 PM, Wednesday, 13 September 2006 Moscone Center -- Room 307, Oral
Division of Inorganic Chemistry |