BIOMIMETIC MODELING OF THE ACTIVE SITE OF [FE]-HYDROGENASE

[FE]-氢化酶活性位点的仿生建模

• 批准号: 8362245
• 负责人: Robert Karoly Szilagyi
• 金额: $ 1.26万
• 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/8362245
• 关键词: Active Sites; Biochemical; Biomimetics; Carbon Monoxide; Data; Electronics; Enzymes; Family; Funding; Grant; Hydrogenase; Life; Ligands; Maps; Measurement; Methods; Modeling; Molecular; National Center for Research Resources; Organism; Oxidoreductase; Principal Investigator; Radiation; Research; Research Infrastructure; Resources; Series; Source; Structure; Uncertainty; United States National Institutes of Health; Work; absorption; cost; electronic structure; iron hydrogenase; nickel-iron hydrogenase; structural biology

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. Recent biochemical work by Thauer allowed for the structural characterization of the active site in [Fe]-hydrogenase. This hydrogenase is unique in a sense that it does not contain Fe-S clusters like the [FeFe]- and the [NiFe]-hydrogenases. However, it shows a common active site structural motif for the presence of diatomic ligands which is likely carbon monoxide. The hydrogenases are the only family of enzymes that contain this otherwise toxic ligand to living organisms. We are proposing a series of multi-edge x-ray absorption measurements to fully characterize the electronic and geometric structure of several biomimetic compounds. Our data will allow for the refinement of several uncertainties with the active site in composition, electronic, and geometric structure. Furthermore, the XANES and EXAFS data will allow us to validate electronic structure calculation methods that are to be used to map the molecular mechanism of the H2-forming methylenetetrahydromethanopterin dehydrogenase.

该副本是利用资源的众多研究子项目之一 由NIH/NCRR资助的中心赠款提供。对该子弹的主要支持 而且，副投影的主要研究员可能是其他来源提供的 包括其他NIH来源。 列出的总费用可能 代表subproject使用的中心基础架构的估计量， NCRR赠款不直接向子弹或副本人员提供的直接资金。 Thauer最近的生化工作允许在[Fe]氢化酶中进行活性位点的结构表征。从某种意义上说，这种氢酶是独一无二的，它不包含[Fefe]和[Nife] - 氢化酶之类的Fe-S簇。然而，它显示出一种可能是一氧化碳的双原子体配体的常见活性位点结构基序。氢化酶是唯一含有这种有毒配体的酶家族。我们提出了一系列多边X射线吸收测量值，以完全表征几种仿生化合物的电子和几何结构。我们的数据将允许在组成，电子和几何结构中与活性位点进行几种不确定性的细化。此外，XANES和EXAFS数据将使我们能够验证电子结构计算方法，该方法用于绘制H2形成H2形成的甲基苯二甲酸甲甲基丙捷酶脱氢酶的分子机制。