Molybdenum (Mo) enzymes are required by almost every living organism on earth and can be traced back to the “last universal common ancestor (LUCA).” Mo enzymes are crucial to fundamental biochemical reactions, such as respiration, protein synthesis, detoxification, as well as the global cycling of the elements carbon, nitrogen and sulfur. At the active site of Mo enzymes is the molybdenum cofactor (Moco), which is composed of a molybdenum metal center and one or two pterin-dithiolene ligands. The Burgmayer lab has synthesized multiple model systems that are similar in structure to the biological Moco to explore different chemical properties possessed by Moco, including the redox potentials of the pterin. The work to be presented includes a description of the general synthesis of one of the current pterin-dithiolene models with a fully reduced pterin, as well as the model’s various properties, including its stereoisomers, its stability in air, in the presence of acidic environment, and in changing temperature. The target model system is generally described as [TEA][Tp*Mo(O)(S2C2(pterin)(-C(CH3)2OH)] (1), where TEA is tetraethylammonium, and Tp* is tris(3,5-dimethylpyrazolyl)hydroborate.

Chemical properties of modeled molybdenum cofactor

ACS Spring 2022

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