LOW TEMPERATURE RAMAN SPECTROSCOPY OF MODEL METALLOENZYME ACTIVE SITES

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 研究工作旨在设计、合成和光谱分析可溶性甲烷单加氧酶(SMMO)的羟基酶成分的小分子类似物，sMMO是一种将甲烷氧化为甲醇的细菌双铁酶。这些模拟研究的最终目的是重现和理解sMMO的反应性。在过去的一年里，人们合成并研究了几种低温下与氧气反应的sMMO羟基酶组分的结构模型。利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.