STUDIES ON ENZYMES INVOLVED IN THE GLOBAL CYCLING OF HYDROGEN, NITROGEN AND CARB

参与氢、氮和碳水化合物全球循环的酶的研究

• 批准号: 7954345
• 负责人: JOHN W PETERS
• 金额: $ 0.75万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2009
• 资助国家: 美国
• 起止时间: 2009-03-01 至 2010-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7954345
• 关键词: Address; Alkenes; Biochemical; Catalysis; Computer Retrieval of Information on Scientific Projects Database; Enzymes; Funding; Goals; Grant; Hydrogen; Hydrolysis; Individual; Institution; Ketones; Methods; Nitrogen; Pathway interactions; Production; Reaction; Research; Research Personnel; Resolution; Resources; Source; Structure; United States National Institutes of Health; base; enzyme mechanism; enzyme structure; novel; phosphate ester; programs; research study; structural biology; synchrotron radiation

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 following program proposal narrative describes individual experiments for several projects that involve the use of synchrotron radiation for structure determination using x-ray diffraction methods to address problems concerning the mechanism of enzyme catalyzed reactions. Toward these ends, we are determining the structure of novel enzymes and utilizing information obtained by previous biochemical and biophysical studies as a basis for capturing and determining the structure of enzymes in defined states that mimic intermediates along the pathway of catalysis. The overall goal of these studies is to utilize the structures of defined states of certain enzymes to contribute to the overall understanding of enzyme mechanism and therefore there is significant value in conducting these studies at high resolution. We are currently pursuing these studies for enzymes involved in hydrogen production, nitrogen reduction, phosphate ester hydrolysis, and bioconversion of alkenes and ketones.

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 下面的项目建议叙述描述了几个项目的个别实验，这些项目涉及使用同步辐射进行结构测定，使用X射线衍射方法来解决有关酶催化反应机制的问题。 为了实现这些目标，我们正在确定新酶的结构，并利用以前的生物化学和生物物理学研究所获得的信息作为捕获和确定酶结构的基础，这些酶在定义的状态下模仿催化途径沿着的中间体。 这些研究的总体目标是利用某些酶的定义状态的结构，以促进对酶机制的全面理解，因此在高分辨率下进行这些研究具有重要价值。 我们目前正在进行这些研究的酶参与氢的生产，氮还原，磷酸酯水解，烯烃和酮的生物转化。