LOW TEMPERATURE RAMAN SPECTROSCOPY OF MODEL METALLOENZYME ACTIVE SITES

这个子项目是利用由NIH/NCRR资助的中心拨款提供的资源的许多研究子项目之一。子项目和调查员(PI)可能从另一个NIH来源获得了主要资金，因此可能会出现在其他CRISE条目中。列出的机构是针对中心的，而不一定是针对调查员的机构。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.