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Updated: May 12, 2026

Sequence-specific Labeling of Nucleic Acids and Proteins with Methyltransferases and Cofactor Analogues
Published on: November 22, 2014
Replica of a fishy enzyme: structure-function analogue of trimethylamine-N-oxide reductase
Golam Moula1, Moumita Bose, Sabyasachi Sarkar
1Department of Chemistry, Indian Institute of Technology, Kanpur, Kanpur-208016, Uttar Pradesh, India.
Abstract:
Three new complexes, [Mo(IV)O(mnt)(SS)](2-) (SS = dimethylethylenedicarboxylate (DMED), toluenedithiolate (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 trimethylamine-N-oxide ((CH3)3N(+)-O(-) or TMANO), the biological substrate of trimethylamine-N-oxide reductase, to trimethylamine ((CH3)3N), responsible for the fishy smell of dead aquatic animals. The reaction kinetics of trimethylamine-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.
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