Investigation of solvent effect on the active site energy of Carbonic Anhydrase and Ribonucleotide Reductase

Subject Areas : Journal of Physical & Theoretical Chemistry

M. Heshmat ¹ , S. Saki ² , M. Khaleghian ³ , S. Irani ⁴ , M. Monajjemi ⁵

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Received: 2015-05-09 Accepted : 2015-05-09 Published : 2008-05-01

Keywords: Enzyme, Basis sets, dipole moment,

Abstract :

Enzymes catalyze many biological reactions. The rates of chemical reaction in the presence ofenzymes are, in some cases, accelerated more than 10 orders of magnitude relative to thecorresponding rates in solution.In this paper a comparison between optimized structures of two enzyme molecules in aspect ofenergy and dipole moment in different conditions including presence of metallic ion, withoutmetallic ion and in the presence of substrate molecule was performed. The stabilizing effect ofmetallic ion is clearly seen. The calculations were performed with three basis sets: 6-31G, 6-31G*and 6-31G** and 6 different solvents and in vacuum. We conclude that the addition of polarizedfunctions to basis sets cause to create higher energy level of system.