Table of Contents
Journal of Computational Medicine
Volume 2013, Article ID 312183, 5 pages
Research Article

Molecular Docking Study on the Interaction of Riboflavin (Vitamin ) and Cyanocobalamin (Vitamin ) Coenzymes

1Biophysics Research Unit, Department of Biochemistry, University of Karachi, Karachi 75270, Pakistan
2International Center for Biological and Chemical Sciences, HEJ Research Institute of Chemistry, University of Karachi, Karachi 75270, Pakistan
3Biomedical Engineering Department, NED University of Engineering and Technology, Karachi 75270, Pakistan

Received 14 November 2012; Revised 25 February 2013; Accepted 13 March 2013

Academic Editor: Rocky Goldsmith

Copyright © 2013 Ambreen Hafeez et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


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