title: A combined approach of experiments and computational docking simulation to the Coprinus cinereus peroxidase-catalyzed oxidative polymerization of alkyl phenols.
abstract: The characteristics of the oxidative polymerization of alkyl phenol derivatives catalyzed by Coprinus cinereus peroxidase (CIP) were studied qualitatively and quantitatively using a combined approach of experiments and computational docking simulations. As determined by docking study of CIP and alkyl phenols, the binding interaction was found to be important for the determination of substrate specificity. The distant binding and indirect orientation of o-isopropyl phenol and o-tertiary butyl phenol to the catalytic residue (56His) could explain the inability of CIP to polymerize these substrates. Three hydrophobic residues (156Pro, 192Leu, and 230Phe) at the entrance of the binding pocket were also found to be crucial in binding and orientation of alkyl phenols. A two-parameter QSAR equation with the binding distance and the molecular volume of the substrates was proposed and the polymerization yield was accurately predicted by two-parameter QSAR equation.
authors.affiliation: School of Chemical and Biological Engineering, Seoul National University, Seoul 151-744, Republic of Korea.
authors.forename: Jong Chul
authors.initials: JC
authors.lastname: Park
authors.forename: Jeong Chan
authors.initials: JC
authors.lastname: Joo
authors.forename: Eun Suk
authors.initials: ES
authors.lastname: An
authors.forename: Bong Keun
authors.initials: BK
authors.lastname: Song
authors.forename: Yong Hwan
authors.initials: YH
authors.lastname: Kim
authors.forename: Young Je
authors.initials: YJ
authors.lastname: Yoo
mesh_terms: D003198:Computer Simulation; D003302:Coprinus / Q000201:enzymology*; D008956:Models, Chemical; D010084:Oxidation-Reduction; D009195:Peroxidase / Q000378:metabolism*; D010636:Phenols / Q000378:metabolism*; D058105:Polymerization; D021281:Quantitative Structure-Activity Relationship
chemical_list: D010636:Phenols; D009195:Peroxidase