OXIDATION REACTIVITY IN SMALL METAL COMPLEXES

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Movement of unique biological catalytic reactivity to small synthetic molecules, while a formidable challenge, is an extremely intriguing and informative endeavor providing critical insights into the native reactivity. The broad and long-term objective of our research is elucidation of the structural and electronic properties of Cu-dioxygen species formed in biological mononuclear, binuclear and trinuclear Cu-sites and subsequent characterization of their oxidative reactivity. Additional studies are directed to understand the mononuclear iron and manganese containing enzymes that oxidize organic substrates. The methodology is that of the synthetic analog approach to the active sites of metallobiomolecules, whereby low molecular weight complexes are synthesized and examined at a small molecule level of detail to reveal intrinsic properties of the metal complexes uncoupled from the influences of the protein matrix. Our premise is that the formation and subsequent reactivity of biological intermediates should be reproducible in small synthetic complexes if appropriate ligation environments are engineered, and if deleterious bimolecular reactions of the reactive intermediates are avoided. Creation of spectroscopically congruent, functional models is the ultimate goal so that specific aspects of proposed biological mechanisms may be investigated at a small molecule level of detail.