Abstract: Yichun Fu
Mentor: Dr. Sharon Burgmayer
The pterin dithiolene ligand plays an important role in the biochemical functions of the molybdenum cofactor due to its ability to transfer electrons and store charges. The pterin-dithiolene molybdenum complex, has various redox paths that contribute to its multiple functions for the enzyme. Studying the forms and interchange of the molyndenum pterin-dithiolene complexes at different oxidation states offers a better understanding of the mechanism of the molybdenum cofactor.
The goal of this research project is to study the characteristics of BMOPP pterin dithiolene complexes, to conduct the conversions of its different oxidation states and to improve the yield and purity. Previous study by the Burgmayer Lab showed a clear pathway of the synthesis of BMOPP dithiolene compound TEA[Tp*Mo4+(S)S2BMOPP]; however, further experiments are needed to optimize the isolation of TEA[Tp*Mo4+(S)S2BMOPP], and its oxidized version Tp*Mo5+(S)S2BMOPP. The next goal is to separate and isolate TEA[Tp*Mo5+(O)S2BMOPP] and Tp*Mo5+(O)(pyrano-S2BMOPP) using TLC and chromatography techniques. The conversion, isolation, and characterization of “806”, a reduced TEA [Tp*Mo4+(O)(H2-S2BMOPP)] is also studied with suitable NMR techniques.
The conversion demonstrates the abundant redox capabilities of the system, and helps to understand how the electron transfer occurs, and its importance in the enzyme. All the reactions are conducted in the dry-box to prevent the deterioration of the compounds. ESI-MS and TLC are used throughout the experiment to monitor the reactions. Cyclic voltammetry is also used to determine the characteristics of the complexes.
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