A.K. Banerjee

Bio: A.K. Banerjee is an academic researcher. The author has an hindex of 1, co-authored 1 publications receiving 14 citations.

Oxo-Mo(IV)(dithiolene)thiolato complexes: analogue of reduced sulfite oxidase.

Abstract: A series of [MoIVO(mnt)(SR)(N–N)]− (mnt = maleonitriledithiolate; R = Ph, nap, p-Cl-Ph, p-CO2H-Ph, and p-NO2-Ph; N–N = 2,2′-bipyridine (bipy) and 1,10-phenanthroline (phen)) complexes analogous to the reduced active site of enzymes of the sulfite oxidase family has been synthesized and their participation in electron transfer reactions studied. Equatorial thiolate and dithiolene ligations have been used to closely simulate the three sulfur coordinations present in the native molybdenum active site. These synthetic analogues have been shown to participate in electron transfer via a pentavalent EPR-active Mo(V) intermediate with minimal structural change as observed electrochemically by reversible oxidative responses. The role of the redox-active dithiolene ligand as an electron transfer gate between external oxidants and the molybdenum center could be envisaged in one of the analogue systems where the initial transient EPR signal with ⟨g⟩ = 2.008 is replaced by the appearance of a typical Mo(V)-centered EP...