Inspired by the unusual active site structures and reactivities exhibited by copper enzymes, we seek to prepare and characterize synthetic complexes in order to test hypotheses developed to explain the novel functions of the biological sites. In collaborative work with Klaus Theopold, comparisons were drawn about the nature of O-O bonding in a variety of side-on metal-dioxygen adducts relevant to postulated intermediates in oxidation catalysis. Aspects of this work will be reviewed, and key lessons learned from correlations of O-O stretching frequencies and X-ray crystallographic data will be presented.

O-O bonding in metal-dioxygen adducts

247th National Meeting (2014)

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