STRUCTURE-FUNCTION RELATIONSHIPS IN FE- AND CO-CONTAINING NITRILE HYDRATASES

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。 本研究的总体目标是利用X射线吸收光谱分析氰基水合酶(NHASS)的反应机理。在工业上广泛使用氰化物来生产含胺、羧酸、酯、醛、酮和杂环化合物的各种特种化学品，凸显了该项目的重要性。这些化合物用于广泛的化学反应，作为生产溶剂、萃取剂、药品、农药和聚合物的原料。本研究旨在明确嗜热假单胞菌JCM 3095的Co型氰基水合酶(PtNHase)和酮单胞菌的Fe型NHase(CtNHase)的反应机理。这项拟议工作的成功完成不仅将为深入了解NHase酶的催化机理提供依据，也将为NHase酶在有机化工加工、工业合成和生物修复工具中的应用提供新的视角。

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. The overall goal of this research is to use x-ray absorption spectroscopy to analyze the reaction mechanism of nitrile hydratases (NHases). The importance of this project is underscored by the extensive industrial use of nitriles to produce a broad number of specialty chemicals containing amines, amides, amidines, carboxylic acids, esters, aldehydes, ketones, and heterocyclic compounds. These compounds are used in a wide array of chemical reactions as feedstock for the production of solvents, extractants, pharmaceuticals, pesticides, and polymers. The proposed research aims to define the reaction mechanisms for both the Co-type nitrile hydratase from Pseudonocardia thermophila JCM 3095 (PtNHase) and the Fe-type NHase from Comamonas testosteroni (CtNHase). The successful completion of the proposed work will not only provide insight into the catalytic mechanism of NHase enzymes, but will also provide new insight into the use of NHase enzymes in organic chemical processing, industrial syntheses, and bioremediation tools.