LOW TEMPERATURE RAMAN SPECTROSCOPY OF MODEL METALLOENZYME ACTIVE SITES

模型金属酶活性位点的低温拉曼光谱

• 批准号: 7357935
• 负责人: Stephen J. Lippard
• 金额: $ 2.03万
• 依托单位: MASSACHUSETTS INSTITUTE OF TECHNOLOGY
• 依托单位国家: 美国
• 财政年份: 2006
• 资助国家: 美国
• 起止时间: 2006-06-01 至 2007-05-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7357935
• 关键词: Raman spectrometry; adduct; analog; cold temperature; enzymes; metalloenzyme; methane monooxygenase; methanol; model; oxygen; small molecule

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.

该子项目是利用NIH/NCRR资助的中心赠款提供的资源的许多研究子项目之一。子弹和调查员（PI）可能已经从其他NIH来源获得了主要资金，因此可以在其他清晰的条目中代表。列出的机构适用于该中心，这不一定是调查员的机构。研究工作是针对可溶性甲烷单加仑酶（SMMO）的羟化酶成分的小分子类似物的设计，合成和光谱研究，这是一种细菌二烯酶，将甲烷氧化为甲醇。这些建模研究的最终目标是再现和了解SMMO的反应性。在过去的一年中，对在低温下与二恶英反应的SMMO羟化酶成分的几种结构模型进行了合成和研究。共振拉曼光谱被用于表征这些氧加合物。