Metalloproteins are essential for a large number of basic processes of life including photosynthesis, respiration, detoxification against toxic substances, biosynthesis of hormones etc.
Our group is involved in developing artificial thermostable enzymes to catalyze different important chemical reactions. The studies are motivated by challenges of energy storage, and also to develop alternative green chemistry methods for syntheses of important chemicals (eg., dyes, drug precursors etc). We search for the answer to the basic question of (i)what are the key molecular-level interactions in these thermostable enzymes that tunes the catalytic (oxidation/reduction) properties of the the metal ion containing centre at the catalytic active site of these enzymes, and (ii) what is the molecular basis of the observed high-thermostability of these enzymes, while having their structure and amino acid combinations are very similar to known mesophilic enzymes of the same superfamily.
The enzyme systems are based on a thermostable cytochrome P450 cloned in E coli. The group is developing nano-bio catalysts by conjugating the cytochrome P450 enzymes to suitable nanoparticles to efficiently convert hydrocarbons and analogs to their corresponding alcohols using electrochemical or photochemical energy as the driving force.
We also have discovered new copper binding peptides as models for intermediates of the formation of the dinuclear copper center in the respiratory enzyme cytochrome oxidase.