Replica of a Fishy Enzyme: Structure-Function Analogue of Trimethylamine-N-Oxide Reductase

Three new complexes, [(MoO)-O-IV(mnt)(SS)](2-) (SS = dimethylethylenedicarboxylate (DMED), tolueneclithiolate (tdt), benzenedithiolate (bdt); mnt = maleonitriledithiolate), each possessing two different dithiolene ligands, are synthesized as model of trimethylamine-N-oxide reductase. The asymmetric dithiolene ligands present in these complexes simulate the two different (P and Q) pterin coordinations in the family of DMSO reductase. These complexes reduce trirnethylamine-N-oxide ((CH3)(3)N+-O- or TMANO), the biological substrate of trimethylamine-N-oxide reductase, to trimethylamine ((CH3)(3)N), responsible for the fishy smell of dead aquatic animals. The reaction kinetics of trirnethylamine-N-oxide reduction by these complexes follow the Michaelis-Menten saturation kinetics. These experimental findings have been rationalized by DFT, TD-DFT level of calculations.