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Copper-Nitrosyl Complex Unveiled

Chemists characterize a key intermediate in the reduction of NO2 to NO by the enzyme copper nitrite reductase

by Jyllian N. Kemsley
October 11, 2010 | A version of this story appeared in Volume 88, Issue 41

A copper-nitrosyl complex is the first Cu(II)–NO species to be structurally characterized, reports a group led by Trevor W. Hayton of the University of California, Santa Barbara (J. Am. Chem. Soc., DOI: 10.1021/ja105930b). The Cu(II)–NO species is believed to be a key intermediate in the reduction of NO 2 to NO by the enzyme copper nitrite reductase. The enzyme is found in a variety of bacteria and plays a key role in the global nitrogen cycle. The researchers prepared the complex by adding NOPF6 to copper metal powder in nitromethane. Analysis of crystals formed from the resulting deep-purple solution showed that the product is a distorted octahedral copper complex with five CH3NO2 ligands and one NO ligand. The nitrosyl group is bound in a bent geometry and has a Cu–N bond length of 1.955 Å, which is significantly longer than those of other Cu–NO complexes. The Cu(II)–NO complex can transfer NO+ to a variety of substituted benzene compounds. The characterization of the new complex could provide insight into the detailed mechanism of action of copper nitrite reductase, as well as the mechanisms of other NOx reductive processes promoted by copper centers, says bioinorganic chemist William B. Tolman of the University of Minnesota, Twin Cities.


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