LOW TEMPERATURE RAMAN SPECTROSCOPY OF MODEL METALLOENZYME ACTIVE SITES

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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. Research efforts are directed towards the design, synthesis and spectroscopic investigation of small molecule analogs of the hydroxylase component of soluble methane monooxygenase (sMMO), a bacterial diiron enzyme that oxidizes methane to methanol. The ultimate goal of these modeling studies is to reproduce and understand the reactivity of sMMO. Over the past year, several structural models of the hydroxylase component of sMMO that react with dioxygen at low temperature were synthesized and investigated. Resonance Raman spectroscopy was employed to characterize these oxygen adducts.