The DMSO reductase family of enzymes whose Mo-centers are comprised of two inequivalent pyranopterin cofactors. We hypothesize such an assymmetry is due to a difference in the redox states of the cofactors and may aide in tuning the reactivity of the cofactor. This investigation focuses on the synthesis and characterization of oxoMo(dithiolene) complexes with two dithiolene ligands differing in their redox states. These complexes are designed to represent the assymmetry caused by the different redox states of the dithiolene ligand that is also observed in the crystal structures of the DMSO reductase family. This work will present molecules that possess the fully reduced dithiolene ligands, toluene,3,4-dithiol (tdt) and benzene-1,2 dithiol (bdt). Characterization details such as IR, UV visible, and NMR spectroscopic studies as well as structural and electrochemical studies will be presented. Reactivity studies using biologically relevant substrates will also be discussed.

Effects ligand oxidation state have on structure, electronic, and reactivity properties of DMSO reductase models

254th National Meeting (2017)

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