Formate dehydrogenase (FDH) enzymes are known to reversibly convert formate to carbon dioxide. An MVI=S (Mo/W) moiety with two pyranopterindithiolate cofactors and a cysteinate/selenocysteinate is believed to be an active oxidized species capable of reacting with formate (HCO2-) to generate CO2. A variety of plausible mechanisms have been proposed involving hydride transfer from formate and generating MIV-SH/MIV=S species as the reduced analogues. Biomimetic synthetic chemistry and reactivity of this enzyme is the major focus for this work. Redox chemistry of Mo and W was explored in the presence of bidentate dithiocarbamate ligand as mimics of pyranopterindithiolate. In particular, significant efforts were made to synthesize WVI=S complexes in the sulfur-rich dithiocarbamate environment. The reactivity of a WVI=S complex in the presence of various hydride sources including formate were explored, and the products were characterized by spectroscopic and crystallographic techniques. Additionally, diamido-dithiolate containing tetra- and pentadentate ligands are currently being investigated as more robust frameworks to support WVI=S/WIV-SH chemistry.

Efforts towards synthesis and reactivity of biomimetic model complexes of formate dehydrogenases

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ACS Fall 2022

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