A large number of chemical reactions are catalyzed by flavoenzymes- a group of enzymes that utilizes flavin ring as a cofactor. The versatility arises mainly due to the ability of enzyme matrix to modulate flavin's redox potentials by altering non-covalent interactions. These interactions include hydrogen bonding with flavin ring atoms, hydrophobic interactions due to aromatic side chains, and p-p stacking interactions with aromatic substrates (e.g. quinone reductases).  Although, recent theoretical studies were successful to model hydrogen bonding interactions,1-2 the effects of aromatic interactions on the redox properties of flavins have remained only partially revealed. The difficulty in modeling these interactions arises because of limitations in various theoretical treatments to reproduce van der Waal's interactions. In the present study, the p-p stacking interactions of flavin and other aromatic molecules have been studied using improved semi-empirical and density functional theories. The effect of these aromatic interactions on binding as well as catalysis will be presented.  Bibliography (1)   Rauschnot, J. C.; Yang, C.; Yang, V.; Bhattacharyya, S. J. Phys. Chem. B 2009 , 113, 8149-8157(2)   Mueller, R. M., North, M. A., Yang, C., Hati, S., Bhattacharyya, S. J. Phys. Chem. B 2011 , 115, 3632-3641.

Quantum chemical studies of the binding and catalytic hydride transfer reaction of flavin with aromatic substrates

245th National Meeting (2013)

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