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Int. J. Mol. Sci. 2005, 6(9), 245-256; doi:10.3390/i6090245
Article

Inhibition of Heme Peroxidase During Phenol Derivatives Oxidation. Possible Molecular Cloaking of the Active Center

1,2,*  and 1
1 Vytautas Magnus University, Vileikos 8, 44404, Kaunas, Lithuania 2 Institute of Biochemistry, Mokslininku 12, 08662 Vilnius, Lithuania
* Author to whom correspondence should be addressed.
Received: 1 March 2005 / Accepted: 29 August 2005 / Published: 20 October 2005
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Abstract

Ab initio quantum chemical calculations have been applied to the study of the molecular structure of phenol derivatives and oligomers produced during peroxidasecatalyzed oxidation. The interaction of substrates and oligomers with Arthromyces ramosus peroxidase was analyzed by docking methods. The most possible interaction site of oligomers is an active center of the peroxidase. The complexation energy increases with increasing oligomer length. However, the complexed oligomers do not form a precise (for the reaction) hydrogen bonding network in the active center of the enzyme. It seems likely that strong but non productive docking of the oligomers determines peroxidase inhibition during the reaction.
Keywords: Ab initio; docking; peroxidase; phenol; oligomer Ab initio; docking; peroxidase; phenol; oligomer
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).
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Ziemys, A.; Kulys, J. Inhibition of Heme Peroxidase During Phenol Derivatives Oxidation. Possible Molecular Cloaking of the Active Center. Int. J. Mol. Sci. 2005, 6, 245-256.

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