Study of molecular basis of interaction between b12 enzymes and flavin derivatives using molecular docking technique

The kinetic studies indicate that riboflavin acts as a sensitizer in the photolysis of cyanocobalamin and in this way promotes the degradation of the molecule. Many microorganisms use light for pathogenesis.The present work describes the interaction of vitamin B2 and B12 at molecular level in bacterial enzymes which could delineate the possible mechanism of inhibiting the disease producing bacteria. Methodology: The molecular basis of interaction between the flavin derivatives and the B12- dependent enzymes was studied using molecular modeling software, the MVD. A series of nineteen flavin derivative sand three B12 containing enzymes; glutamate mutase, diol dehydratase and methionine synthase were taken for the study. The potential binding affinity between flavin derivatives and B12 enzymes was checked on the basis of lowest docking score, number of hydrogen bonds and favorable binding modes. Results: We found riboflavin, 2-ketoflavin and 4-ketoflavin as the best interacting compounds with each of the three enzymes taken. The regions containing lone pair of electrons are critical for the maximum number of binding conformations. Conclusion: It may be concluded that flavin derivatives may influence the activity of B12 enzymes. Therefore,the understanding of molecular basis of this interaction and the identification of the key factors involved,might be useful to design new molecules with enhanced selectivity towards B12 dependent enzymes. Thi scan lead to the screening and discovery of new compounds as useful antibiotics and the active natural drugs. (author)