Spectroscopic and Electronic Structure Studies of Symmetrized Models for Reduced Members of the Dimethylsulfoxide Reductase Enzyme Family

Abstract

Enzymes belonging to the dimethylsulfoxide reductase (DMSOR) family of pyranopterin Mo enzymes have a unique active-site geometry in the reduced form that lacks a terminal oxo ligand, unlike the reduced active sites of other pyranopterin Mo enzymes. Furthermore, the DMSOR family is characterized by the coordination of two pyranopterin-ene-1,2-dithiolate ligands in their active sites, which is distinctive among the other pyranopterin Mo enzymes but analogous to all of the currently known tungsten-containing enzymes. Electronic absorption, resonance Raman, and ground- and excited-state density functional calculations of symmetrized analogues of the reduced DMSOR active site ([NEt4][Mo(IV)(QAd)(S2C2Me2)2] where Ad = 2-adamantyl; Q = O, S, Se) have allowed for a detailed description of Mo-bisdithiolene electronic structure in the absence of a strong-field oxo ligand. The electronic absorption spectra are dominated by dithiolene S --> Mo charge-transfer transitions, and the totally symmetric Mo-S Raman stretch is observed at approximately 400 cm(-1) for all three complexes. These data indicate that the Mo-bisdithiolene bonding scheme in high-symmetry [Mo(QAd)(S2C2Me2)2]- complexes is not strongly perturbed by the apical QAd- ligands, but instead, the dithiolene ligands define the t(2g) ligand field splitting. The effects of conserved geometric distortions observed in DMSOR, relative to these high-symmetry models, were explored by spectroscopically calibrated bonding calculations, and the results are discussed within the context of electronic structure contributions to ground-state destabilization and transition-state stabilization. The specific electronic structure tuning of the endogenous amino acid ligation on the mechanism of DMSOR is also discussed.