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Selected Publication:

Kirchner, T; Flemmig, J; Furtmüller, PG; Obinger, C; Arnhold, J.
(2010): (-)-Epicatechin enhances the chlorinating activity of human myeloperoxidase.
Arch Biochem Biophys. 2010; 495(1):21-27 FullText FullText_BOKU

The heme-containing enzyme myeloperoxidase (MPO) accumulates at inflammatory sites and is able to catalyse one- and two-electron oxidation reactions. Here it is shown that (-)-epicatechin, which is known to have numerous beneficial health effects, in low micromolar concentration enhances the degradation of monochlorodimedon (MCD) or the chlorination of taurine in a concentration-dependent bell-shaped manner whereas at higher concentrations it sufficiently suppresses the release of hypochlorous acid. Presented reaction mechanisms demonstrate the efficiency of micromolar concentrations of the flavan-3-ol in overcoming the accumulation of compound II that does not participate in the chlorination cycle. in case of MCD the mechanism is more complicated since it also acts as peroxidase substrate with very different reactivity towards compound 1 (3 x 10(5) M-1 s(-1)) and compound II (8.8 M-1 s(-1)) at pH 7. By affecting the chlorinating activity of myeloperoxidase (-)-epicatechin may participate in regulation of immune responses at inflammatory sites. (C) 2009 Elsevier Inc. All rights reserved.
Authors BOKU Wien:
Furtmüller Paul Georg
Obinger Christian
Find related publications in this database (using NML MeSH Indexing)
Catechin - pharmacology
Cyclohexanones - metabolism
Halogenation - drug effects
Humans -
Peroxidase - metabolism
Taurine - analogs & derivatives

Find related publications in this database (Keywords)
Chlorinating activity

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