Cobalamins are the largest and structurally complex cofactors found in biological systems and have attracted considerable attention\r\ndue to their participation in the metabolic reactions taking place in humans, animals, and microorganisms. Riboflavin (vitamin B2)\r\nis a micronutrient and is the precursor of coenzymes, FMN and FAD, required for a wide variety of cellular processes with a key\r\nrole in energy-based metabolic reactions. As coenzymes of both vitamins are the part of enzyme systems, the possibility of their\r\nmutual interaction in the body cannot be overruled. A molecular docking study was conducted on riboflavin molecule with B12\r\ncoenzymes present in the enzymes glutamate mutase, diol dehydratase, and methionine synthase by using ArgusLab 4.0.1 software\r\nto understand the possible mode of interaction between these vitamins. The results fromArgusLab showed the best binding affinity\r\nof riboflavin with the enzyme glutamate mutase for which the calculated least binding energy has been found to be -7.13 kcal/mol.\r\nThe results indicate a significant inhibitory effect of riboflavin on the catalysis of B12-dependent enzymes. This information can be\r\nutilized to design potent therapeutic drugs having structural similarity to that of riboflavin.
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