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김용환

Kim, Yong Hwan
Enzyme and Protein Engineering Lab.
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A combined approach of experiments and computational docking simulation to the Coprinus cinereus peroxidase-catalyzed oxidative polymerization of alkyl phenols

Author(s)
Park, Jong ChulJoo, Jeong ChanAn, Eun SulSong, Bong KeunKim, Yong HwanYoo, Young Je
Issued Date
2011-04
DOI
10.1016/j.biortech.2010.12.021
URI
https://scholarworks.unist.ac.kr/handle/201301/20374
Fulltext
http://www.sciencedirect.com/science/article/pii/S0960852410019516
Citation
BIORESOURCE TECHNOLOGY, v.102, no.7, pp.4901 - 4904
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.
Publisher
ELSEVIER SCI LTD
ISSN
0960-8524

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