EXAFS OF THE NOVEL HETERO-BINUCLEAR CENTER OF RIBONUCLEOTIDE REDUCTASE FROM C T

来自 C T 的新型核糖核苷酸还原酶异双核中心的 EXAFS

• 批准号: 8362315
• 负责人: MICHAEL T. GREEN
• 金额: $ 0.8万
• 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/8362315
• 关键词: Anti-Bacterial Agents; Antibiotics; Chlamydia trachomatis; Coupled; Development; Electron Transport; Escherichia coli; Funding; Grant; Human; Mycobacterium tuberculosis; National Center for Research Resources; Organism; Principal Investigator; Protons; Radiation; Research; Research Infrastructure; Resources; Ribonucleotide Reductase; Sequence Analysis; Source; Structure; United States National Institutes of Health; absorption; cofactor; cost; novel; oxidation; pathogen; ribonucleotide reductase M2; structural biology; tyrosine radical

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 R2 subunit of ribonucleotide reductase(RNR) from the human pathogen Chlamydia trachomatis (Ct) features a Mn/Fe heterobinuclear center that initiates proton coupled electron transfer (PCET). This differs from RNRs of other organisms including humans and E. coli which both feature a diiron center and a tyrosine radical to initiate PCET. Sequence analyses indicate other human pathogens, such as Mycobacterium tuberculosis, have Mn/Fe RNRs. The fact that Mn/Fe heterobinuclear centers are incorporated in human pathogens suggests that there may be a window for new antibacterial action. Development of new antibiotics will be aided by a complete understanding of the structure and mechanism of Ct R2. The proposed research seeks to provide extended x-ray absorption fine structure EXAFS) characterizations of the Ct R2 cofactor in its various oxidation states.

这个子项目是许多利用资源的研究子项目之一 由NIH/NCRR资助的中心拨款提供。子项目的主要支持 而子项目的主要调查员可能是由其他来源提供的， 包括其它NIH来源。 列出的子项目总成本可能 代表子项目使用的中心基础设施的估计数量， 而不是由NCRR赠款提供给子项目或子项目工作人员的直接资金。 来自人类病原体沙眼衣原体（Ct）的核糖核苷酸还原酶（RNR）的R2亚基具有启动质子耦合电子转移（PCET）的Mn/Fe异双核中心。这与包括人类和E.大肠杆菌，这两个功能的二铁中心和酪氨酸自由基启动PCET。序列分析表明，其他人类病原体，如结核分枝杆菌，具有Mn/Fe RNR。Mn/Fe异双核中心被纳入人类病原体的事实表明，可能有一个新的抗菌作用的窗口。新抗生素的开发将有助于对Ct R2结构和机制的全面了解。所提出的研究试图提供Ct R2辅因子在其各种氧化态下的扩展X射线吸收精细结构EXAFS表征。