Author(s)

Srijita Basumallick^1,2, T. N. Guru Row¹

¹Solid State Chemistry and Structural Unit, Indian Institute of Science, Bangalore, India.
²Department of Chemistry, National Institute of Technology, Agartala, India.

Tans-Atovaquone is widely used as an effective drug to treat uncomplicated malaria. But its cis-isomer is not a drug. In the present study, we report energy minimized binding pattern of trans-Atovaquone and its cisisomer with cytochrome bc1 (cytbc1) of yeast. The new feature of this molecular docking computation is that structural parameters of the drug molecules have been determined from their crystal structures. The energy minimized structures of protein-drug complexes show that H-bond distant between His-181 of cytochrome bc1 and C=O of Atovaquone for trans-Atovaquone is 2.85 Å and 5.3 Å with the cis-isomer. The role of this H-bonding interaction in dictating drug potency is in conformity with proton-coupled electron transport mechanism of drug action.

Anti-Malarial Drug, Crystal Structures, Atovaquone, Docking-Studies

Basumallick, S. and Row, T. (2015) Binding Study of Cis-Atovaquone with Cytochrome bc1 of Yeast. Computational Molecular Bioscience, 5, 57-63. doi: 10.4236/cmb.2015.54007.