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

Auburn University, Auburn AL

Investigators

Abstract

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.