Research Interests:

Our research focused to understand the intrinsic properties of metal ions in certain ligand donor environments, mimicking biological metal active sites. We synthesize the targeted complexes of mainly Cu and Ni ions in N, S donor coordination environment and study their electronic properties by means of various spectroscopic methods including X-ray structure determination. The spectroscopic measurements include: FT-IR, 1H NMR, UV-Vis, UV-Vis-NIR, cyclic voltammetry, EPR, fluorescence, ESI Mass and others if required. Spectro-electrochemistry plays a vital role to study (a) the nature of redox reactions and (b) the stability of metal oxidation states involved to show the reactivity with small molecules.

We have successfully contributed little bit to the Modelling work of biological (a) Copper active sites of few copper containing enzymes such as: Copper Nitrite Reductase, CuM site of Hydroxylases (i.e. Dopamine-beta-monoxygenase), Copper-Zinc Superoxide Dismutase, CuA & CuZ sites (of Cytochrome-c-Oxidase,  and Nitrous Oxide Reductase) and (b) Nickel active sites of enzymes such as Ni containing Superoxide Dismutase , the NiP Site of Carbonmonoxide Dehydrogenase/Acetyl-Coenzyme A Synthase (CODH/ACS) and the key step of the catalytic cycle of Methyl-Coenzyme M Reductase (MCR).   We usually investigate the reactivity of small molecules such as Nitric Oxide (NO), Carbon Monoxide (CO), Dioxygen (O2), Superoxide Radical Anions (O2.-) with the synthesized model complexes. These reactivity studies are highly important, help to elucidate the mechanism of catalytic action and the role of metal active sites of the enzymes in biology.