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ISSN: 2329-6674

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Editorial

Study of Interaction between Complexes of Copper (II) and Melanin Pigment by Molecular Modeling

Lebbad Fatima11, M Merad1, Nouria Boussalah1, Said Ghalem1, Nasimudeen R Jabir2 and
Mohammad A. Kamal2*
1Laboratoire des Substances Naturelles et Bioactives “LASNABIO” University of Tlemcen, BP 119, 13000, Tlemcen, Algéria
2Metabolomics & Enzymology Unit, Fundamental and Applied Biology Group, King Fahd Medical Research Center, King Abdulaziz University, P. O. Box 80216, Jeddah 21589, Saudi Arabia
Corresponding Author : Mohammad A. Kamal
Metabolomics & Enzymology Unit
Fundamental and Applied Biology Group
King Fahd Medical Research Center
King Abdulaziz University, P. O. Box 80216
Jeddah 21589, Saudi Arabia
Fax: 1501636-8847
E-mail: [email protected]
Received November 06, 2012; Accepted November 09, 2012; Published November 16, 2012
Citation: Fatima L, Merad M, Boussalah N, Ghalem S, Jabir NR, et al. (2012) Study of Interaction Between Complexes of Copper (II) and Melanin Pigment by Molecular Modeling. Enz Eng 1:e107. doi:10.4172/2329-6674.1000e107
Copyright: © 2012 Fatima L, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

Abstract

Tyrosinase is a metalloenzyme belonging to the group of oxidoreductase enzymes. Like many redox enzymes, copper (Cu) ion is present in its active site. We designed an in silico study of 8 previously reported complexes of copper, which catalyze the oxidation reaction of catechol ortho-quinone with different re-activities by calculating steric energies using EMO and Gaussian09 program. The catalytic activity of these complexes depends on several factors such as size of the side chain hydroxyl group. These interesting results could lead to new developments in synthetic biochemistry such as generating more stable conformers.

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