New catalytic functions for [4Fe-4S] clusters

这项无机、生物无机和有机金属化学项目以及分子和细胞生物学项目的研究奖支持阿拉巴马州奥本大学的 Eduardus (Evert) C. Duin 教授的工作，以探讨 1-脱氧-D-木酮糖-5-磷酸 (DOXP) 途径中倒数第二个和最终蛋白质 GcpE 和 LytB 的反应机制，以及它们的活性位点铁硫簇在此过程中的作用。过程。动力学实验将深入了解几种瞬时 EPR 活性物质在反应机制中的作用。将使用 EPR/ENDOR 光谱和基质结构中选定原子的同位素标记相结合来表征该物种。此外，通过底物调节研究将获得有关酶机制的更多细节。综合数据将提供对 GcpE 和 LytB 酶机制的完整理解。由于这两种酶似乎都参与了一种全新类型的催化，这将是对铁硫领域的重要贡献。此外，这些知识将通过提高商业上感兴趣的类异戊二烯的生产难度以及开发对人类危害较小的新型除草剂来有利于生物技术的商业化。该资金还通过购买快速混合/快速冷冻研究设备来支持生物化学部门的研究和教学工作。

This Research award in the Inorganic, Bioinorganic and Organometallic Chemistry program and the Molecular and Cellular Biology program supports work by Professor Eduardus (Evert) C. Duin at Auburn University, Alabama, to probe the reaction mechanism of the penultimate and ultimate proteins in the 1-deoxy-D-xylulose-5-phosphate (DOXP) pathway, GcpE and LytB, and the role of their active-site iron-sulfur clusters in this process. Kinetic experiments will provide insight in the role of several transient EPR-active species in the reaction mechanisms. The species will be characterized using the combination of EPR/ENDOR spectroscopies and isotopic labeling of selected atoms in the substrate structures. In addition further details on the mechanisms of the enzymes will be obtained through substrate modulation studies. The combined data will provide a complete understanding of the mechanisms of the GcpE and LytB enzymes. Since both enzymes seem to be involved in a completely new type of catalysis this will be an important contribution to the iron-sulfur field. In addition, this knowledge will benefit the commericialization of biotechnology through increased ease of production of commercially interesting isoprenoids and the development of novel herbicides that are less harmful to humans. The funding also supports the Biochemistry division research and teaching efforts through the acquisition of equipment for rapid-mix/rapid freeze studies.