Mentor: Professor Sharon Burgmayer
Molybdenum enzymes have important functions across life forms. The enzymes are involved in oxidation and reduction reactions. A lack of molybdenum enzymes can be very dangerous. The active site of the enzyme is known as the Molybdenum Cofactor (Moco). The cofactor consists of a dithiolene group substituted with a pterin moiety, known as molybdopterin, complexed with molybdenum. Attempts to isolate Moco have not been accomplished due its instability outside the enzyme. Therefore, Moco must be studied by building compounds modeled after it. The synthesizing of model Moco compounds has been a major focus of the Burgmayer lab.
A key to building the model is the synthesis of pterin compounds. A precursor of to the syntheses of different model molybdopterins is 6-chloropterin. Traditionally, 6-chloropterin has been made in the lab following a five step process. A disadvantage to this pathway is that the first step is costly and low yielding. This summer along with repeatedly completing this pathway, I will also test out a new proposed pathway. Most of the reactions of the pathway have been studied before. The reaction that will require the most attention is shown in Figure I. My goal for working with this new pathway is to improve its efficiency and the yields of its reactions.