A structural hybrid melding aspects of the active sites of two prominent biological oxygen activation catalysts: binuclear capabilities (as in many cuproproteins), and a tetraphyrrolic framework (as in heme iron proteins), is proposed as an oxygenase mimic. During the evolutionary process the two systems, heme iron and copper proteins, have been closely associated with respect to function; and both copper and heme iron sites are known to occur together in cytochrome oxidase, for example. Thus an examination of the combined influence of these parallel and intertwined systems is an exciting prospect for better understanding the workings of past and potentially future evolutionary processes. Focus will be on the electronic and structural implications of the combined pyrrolic and binuclear ring system on oxygenase activity. Systems to be examined will include the metal ions copper, cobalt, iron, and ruthenium with alkane and olefin substrates. The specific studies to be undertaken will include X-ray crystallographic structural determinations of active catalysts and intermediate species, electrochemical and magnetic studies of the metal ion complexes, and oxygen uptake measurements in conjunction with the isolation and characterization of oxygenated species.
| Sakon, J; Reiter, A; Mertes, K B et al. (1989) Structure of [N,N'-propylenebis(2-pyrrolylmethyleneaminato)]nickel(II). Acta Crystallogr C 45 ( Pt 9):1311-4 |
