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Gewählte Publikation:

Auer, M; Gruber, C; Bellei, M; Pirker, KF; Zamocky, M; Kroiss, D; Teufer, SA; Hofbauer, S; Soudi, M; Battistuzzi, G; Furtmüller, PG; Obinger, C; .
(2013): A stable bacterial peroxidase with novel halogenating activity and an autocatalytically linked heme prosthetic group.
J Biol Chem. 2013; 288(38):27181-27199 FullText FullText_BOKU

Reconstructing the phylogenetic relationships of the main evolutionary lines of the mammalian peroxidases lactoperoxidase and myeloperoxidase revealed the presence of novel bacterial heme peroxidase subfamilies. Here, for the first time, an ancestral bacterial heme peroxidase is shown to possess a very high bromide oxidation activity (besides conventional peroxidase activity). The recombinant protein allowed monitoring of the autocatalytic peroxide-driven formation of covalent heme to protein bonds. Thereby, the high spin ferric rhombic heme spectrum became similar to lactoperoxidase, the standard reduction potential of the Fe(III)/Fe(II) couple shifted to more positive values (-145 +/- 10 mV at pH 7), and the conformational and thermal stability of the protein increased significantly. We discuss structure-function relationships of this new peroxidase in relation to its mammalian counterparts and ask for its putative physiological role.
Autor*innen der BOKU Wien:
Auer Markus
Furtmüller Paul Georg
Grünwald-Gruber Clemens
Hofbauer Stefan
Kroiß Daniela
Obinger Christian
Pirker Katharina
Soudi Monika
Zamocky Marcel
Find related publications in this database (using NML MeSH Indexing)
Bacterial Proteins/chemistry*;Bacterial Proteins/genetics;Bacterial Proteins/metabolism;Bromides/chemistry*;Bromides/metabolism;Cyanobacteria/enzymology*;Cyanobacteria/genetics;Enzyme Stability/physiology;Heme/chemistry*;Heme/genetics;Heme/metabolism;Hydrogen-Ion Concentration;Oxidation-Reduction;Peroxidase/chemistry*;Peroxidase/genetics;Peroxidase/metabolism;

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