Industrial use of chromium leads to the contamination of natural environment with chromium pollution and the hexavalent form is very harmful to the living system compared to the trivalent and other forms. The most sophisticated way of chromium reduction is the use of an enzyme chromate reductase exclusively produced by the bacteria. An insilico sequence and structure analysis of chromate reductase enzyme from three mesophilic bacteria Acetobacter aceti, Escherichia coli, and Pseudomonas putida has been studied. Amino acid variation study indicates a highest number of charged and uncharged residues in P. putida and A. aceti compared to E. coli. Secondary structure analysis indicates that protein from E. coli contains additional beta-hairpin and beta bugle. Higher number of salt bridges, aromatic-aromatic interactions, cation-pi interactions in P. putida chromate reductase provides its more stability then the other two. Molecular dynamics simulation studies through RMSD and RMSF indicates less fluctuation in case of P. putida chromate reductase while lowest Rg indicates tightly packed nature and lower SASA indicates better folding of the said protein. This is the first reporting on structural and sequence analysis of chromate reductase of the three mesophilic bacteria and among them P. putida proved to be the most sable one to be used in the industrial level for better chromate alleviation.

Debanjan Mitra has completed his PhD at the age of 29 years from Raiganj University, India. He is working on bioinformatics specially in the field of proteomics, drug discovery, cheminformatics, quantum mechanics, immunoinformatics and programming. He has published more than 43 papers in reputed journals and has been serving as a reviewer and editorial board member of repute. 1st time he revealed the presence of cyclic salt bridge in protein in the field of structural biology. Till now, he got 6 international and 2 national awards in his scientific life journey.