XAS STUDIES OF COBALAMIN

钴胺素的 XAS 研究

• 批准号: 8170015
• 负责人: SERENA D DE BEER GEORGE
• 金额: $ 0.58万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2010
• 资助国家: 美国
• 起止时间: 2010-05-01 至 2011-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/8170015
• 关键词: Cobalamin; Complex; Computer Retrieval of Information on Scientific Projects Database; Crystallography; Enzymes; Funding; Grant; Institution; Malonyl Coenzyme A; Methionine; Mutase; Nitric Oxide; Proteins; Reaction; Relative (related person); Research; Research Personnel; Resources; Source; Time; United States National Institutes of Health; cofactor; electronic structure

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. Cobalamins are required cofactors in a number of enzyme reactions, including methyl cobalamin-dependent methionine synthase and adensoyl-cobalamin-dependent methyl malonyl-CoA mutase. These enzymes are inhibited by nitric oxide (NO), and it is believed that this is due to the formation of an NO-cobalamin complex. In this proposal, combined XAS, protein crystallography and time-dependent DFT calculations will be used to investigate the geometric and electronic structure of cobalamin-NO relative to that of aqua and methyl cobalamins.

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。 Cobalamins是许多酶反应所需的辅因子，包括依赖于甲钴胺的蛋氨酸合成酶和依赖于腺苷钴胺的甲基丙二酰辅酶A变位酶。这些酶被一氧化氮(NO)抑制，人们认为这是由于NO-钴胺复合体的形成。在该方案中，将结合XAS、蛋白质结晶学和含时密度泛函理论来研究钴胺-NO相对于水和甲基钴胺的几何和电子结构。