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Inhibition mechanism of Tb(III) on horseradish peroxidase activity.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Guo, Shaofen Zhou, Qing Lu, Tianhong Ding, Xiaolan Huang, Xiaohua
Description	Author Affiliation: Guo S ( Jiangsu Key Laboratory of Biofunctional Materials, College of Chemistry and Environmental Science, Nanjing Normal University, Nanjing 210097, P. R. China.)
Abstract	The inhibition mechanism of Tb(III) on horseradish peroxidase (HRP) in vitro was discussed. The results from MALDI-TOF/MS and X-ray photoelectron spectroscopy (XPS) showed that Tb(III) mainly interacts with the O-containing groups of the amides in the polypeptide chains of the HRP molecules and forms the complex of Tb(III)-HRP, and, in the complex, the molar ratio Tb(III)/HRP is 2 : 1. The results from CD and atomic force microscopy (AFM) indicated that the coordination effect between Tb(III) and HRP can lead to the conformation change in the HRP molecule, in which the contents of alpha-helix and beta-sheet conformation in the peptide of the HRP molecules is decreased, and the content of the random coil conformation is increased. Meanwhile, the coordination effect also leads to the decrease in the content of inter- and intrapeptide-chain H-bonds in the HRP molecules, resulting in the HRP molecular looseness and/or aggregation. Thus, the conformation change in the HRP molecules can significantly decrease the electrochemical reaction of HRP and its electrocatalytic activity for the reduction of H2O2.
File Format	HTM / HTML
ISSN	16121872
Issue Number	10
Volume Number	5
e-ISSN	16121880
Journal	Chemistry & Biodiversity
Language	English
Publisher	Wiley
Publisher Date	2008-10-01
Publisher Place	Switzerland
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Biochemistry Discipline Chemistry Enzyme Inhibitors Pharmacology Horseradish Peroxidase Antagonists & Inhibitors Terbium Armoracia Enzymology Dose-response Relationship, Drug Hydrogen Bonding Hydrogen Peroxide Chemistry Oxidation-reduction Protein Binding Thermodynamics Journal Article
Content Type	Text
Resource Type	Article
Subject	Chemistry Medicine Molecular Biology Biochemistry Molecular Medicine Bioengineering

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