Indiana University-Purdue University Indianapolis (IUPUI) / Mononuclear molybdopterin enzymes are a large class of enzymes that are present in all phyla of life. All pterin containing enzymes posses a molybdopterin cofactor made up of a molybdenum metal center coordinated directly by a dithiolene ligand, which is appended to a pyranopterin cofactor. The majority of these enzymes catalyze oxygen atom transfer reactions that are concomitant with a transfer of two-electrons. We are hypothesizing that by altering the oxidation states of the dithiolene, the reactivity of the cofactor can be tuned for different substrates. This investigation focuses on the synthesis and characterization of oxo-MoIV(dithiolene) complexes that possess a fully reduced dithiolene ligand (dithiolene) and a fully oxidized dithiolene ligand (dithione). These complexes are designed to represent the asymmetry of the dithiolene ligand that is observed in the crystal structures of the DMSO reductase family. Asymmetric oxo-MoIV(dithiolene) complexes exhibit a unique structural property, a large fold angle along the S•••S vector of the dithione ligand. These complexes also show a positive solvatochromic effect in a range of polar to nonpolar solvents. The rich electrochemical properties of these redox active complexes and other characterization details such as IR, and NMR studies will be presented. Effects on the reactivity of these complexes using biologically relevant substrates will be discussed. The oxygen atom transfer reactivity has been probed by mass spectrometry and NMR spectroscopy. The presented complexes aide in highlighting the effect redox state of the dithiolene ligand has in modulating reactivity