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

含铁和共基腈水合酶的结构-功能关系

• 批准号: 8362239
• 负责人: ROBERT A SCOTT
• 金额: $ 0.14万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2011
• 资助国家: 美国
• 起止时间: 2011-03-01 至 2012-02-29
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8362239
• 关键词: Aldehydes; Amides; Amidines; Amines; Bioremediations; Carboxylic Acids; Chemicals; Comamonas testosteroni; Enzymes; Esters; Funding; Goals; Grant; Heterocyclic Compounds; Ketones; National Center for Research Resources; Nitriles; Organic Chemicals; Pesticides; Pharmacologic Substance; Polymers; Principal Investigator; Process; Production; Radiation; Reaction; Research; Research Infrastructure; Resources; Solvents; Source; Spectrum Analysis; Structure-Activity Relationship; United States National Institutes of Health; Work; absorption; chemical reaction; cost; insight; medical specialties; nitrile hydratase; structural biology; tool

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. Primary support for the subproject and the subproject's principal investigator may have been provided by other sources, including other NIH sources. The Total Cost listed for the subproject likely represents the estimated amount of Center infrastructure utilized by the subproject, not direct funding provided by the NCRR grant to the subproject or subproject staff. 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.

该子项目是利用资源的众多研究子项目之一 由 NIH/NCRR 资助的中心拨款提供。子项目的主要支持 并且子项目的首席研究员可能是由其他来源提供的， 包括其他 NIH 来源。 子项目可能列出的总成本 代表子项目使用的中心基础设施的估计数量， NCRR 赠款不直接向子项目或子项目工作人员提供资金。 本研究的总体目标是利用X射线吸收光谱分析腈水合酶（NHases）的反应机制。该项目的重要性突显了腈在工业上的广泛用途，以生产多种含有胺、酰胺、脒、羧酸、酯、醛、酮和杂环化合物的特种化学品。这些化合物广泛用于化学反应，作为生产溶剂、萃取剂、药物、农药和聚合物的原料。本研究旨在明确来自嗜热假诺卡氏菌 JCM 3095 的 Co 型腈水合酶 (PtNHase) 和来自睾酮丛毛单胞菌的 Fe 型 NHase (CtNHase) 的反应机制。该工作的成功完成不仅将为NHase酶的催化机制提供深入的见解，而且还将为NHase酶在有机化学加工、工业合成和生物修复工具中的使用提供新的见解。