Table of Contents
ISRN Inorganic Chemistry
Volume 2013 (2013), Article ID 971764, 6 pages
Research Article

Investigation into Structural Changes of the Copper Binding Site in Lysyl Oxidase upon Substrate and Inhibitor Docking

Department of Chemistry and Physics, Emmanuel College, 400 Fenway, Boston, MA 02115, USA

Received 28 May 2013; Accepted 19 June 2013

Academic Editors: F. G. Doro, C. L. Liu, and Z. Xiao

Copyright © 2013 M. Lynch and F. Ryvkin. 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.


The present paper reports a computational investigation of potential communication between the lysine tyrosylquinone (LTQ) and copper cofactors within lysyl oxidase (LOX). Various substrates and inhibitors of LOX were docked into the active site in our computer generated model of the enzyme. Conformational changes in the vicinity of the copper site as well as changes in the electrostatic environment were identified. The appearance of a canal-like structure involving tyrosine 35 (TYR35) and glutamine 104 (GLN104) residues was shown to be consistent upon docking of a variety of different compounds. Interactions between LOX and its natural substrate, collagen, were also explored through molecular dynamic simulations. The possibility of communication between the organic and inorganic cofactors in LOX was proposed, aiding the ongoing debate regarding the role of copper in the catalytic mechanism of this important enzyme.