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Gewählte Publikation:

Jakopitsch, C; Pirker, KF; Flemmig, J; Hofbauer, S; Schlorke, D; Furtmüller, PG; Arnhold, J; Obinger, C; .
(2014): Mechanism of reaction of chlorite with mammalian heme peroxidases.
J Inorg Biochem. 2014; 135:10-19 FullText FullText_BOKU

Abstract:
This study demonstrates that heme peroxidases from different superfamilies react differently with chlorite. In contrast to plant peroxidases, like horseradish peroxidase (HRP), the mammalian counterparts myeloperoxidase (MPO) and lactoperoxidase (LPO) are rapidly and irreversibly inactivated by chlorite in the micromolar concentration range. Chlorite acts as efficient one-electron donor for Compound I and Compound II of MPO and LPO and reacts with the corresponding ferric resting states in a biphasic manner. The first (rapid) phase is shown to correspond to the formation of a MPO-chlorite high-spin complex, whereas during the second (slower) phase degradation of the prosthetic group was observed. Cyanide, chloride and hydrogen peroxide can block or delay heme bleaching. In contrast to HRP, the MPO/chlorite system does not mediate chlorination of target molecules. Irreversible inactivation is shown to include heme degradation, iron release and decrease in thermal stability. Differences between mammalian peroxidases and HRP are discussed with respect to differences in active site architecture and heme modification. (C) 2014 The Authors. Published by Elsevier Inc. This is an open access article under the CC BY-NC-ND license
Autor*innen der BOKU Wien:
Furtmüller Paul Georg
Hofbauer Stefan
Jakopitsch Christa
Obinger Christian
Pirker Katharina
Find related publications in this database (using NML MeSH Indexing)
Animals;Calorimetry, Differential Scanning;Catalytic Domain;Cattle;Chlorides/chemistry*;Electron Spin Resonance Spectroscopy;Heme/chemistry;Horseradish Peroxidase/chemistry;Humans;Kinetics;Lactoperoxidase/chemistry*;Oxidation-Reduction;Peroxidase/chemistry*;Protein Structure, Secondary;Reducing Agents/chemistry*;

Find related publications in this database (Keywords)
Myeloperoxidase
Lactoperoxidase
Chlorite
Hypochlorous acid
Chlorine dioxide
Oxoferin


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