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

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。 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。

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 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.