CRYSTALLOGRAPHIC STUDIES OF METALLOENZYMES

该子项目是利用NIH/NCRR资助的中心赠款提供的资源的许多研究子项目之一。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。所列机构为中心，不一定是研究者所在机构。我们打算获得快速访问时间，继续我们的研究SAM自由基酶和非血红素单核铁蛋白。我们希望通过SAM自由基酶与高度多样化的底物反应来增加我们对5 '-脱氧腺苷自由基的形成和控制的理解。我们还对SyrB 2感兴趣，SyrB 2是一种非血红素单核铁蛋白，它催化生物学上没有先例的氯化物插入反应。我们的快速访问时间将用于解决丙酮酸-甲酸裂解酶活化酶的第一个结构，这是一种最好的生化表征SAM自由基酶，以及SyrB 2，它也尚未进行结构表征。

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. We intend to gain rapid access time to continue our studies of SAM Radical enzymes and non-heme mononuclear iron proteins. We hope to add to our understanding of formation and control of the 5'-deoxyadenosyl radical by SAM Radical enzymes for reaction with highly diverse substrates. We are also interested in SyrB2, a non-heme mononuclear iron protein which catalyzes a chloride insertion reaction without precedent in biology. Our rapid access time will be used to solve the first structures of Pyruvate-formate lyase activase, one of the best biochemically characterized SAM Radical enzymes, as well as SyrB2, which also has not yet been structurally characterized.