LOW TEMPERATURE RAMAN SPECTROSCOPY OF MODEL METALLOENZYME ACTIVE SITES

该子项目是利用 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得主要资金， 因此可以在其他CRISP条目中表示。列出的机构是 中心，不一定是研究者的机构。 研究工作是针对可溶性甲烷单加氧酶（sMMO）的羟化酶组分的小分子类似物的设计，合成和光谱研究，sMMO是一种将甲烷氧化为甲醇的细菌二铁酶。这些建模研究的最终目标是再现和理解sMMO的反应性。 在过去的一年中，几个结构模型的羟化酶的组成部分sMMO反应的分子氧在低温下进行了合成和研究。采用共振拉曼光谱对这些氧加合物进行了表征。

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.