NDLI: A stable bacterial peroxidase with novel halogenating activity and an autocatalytically linked heme prosthetic group.

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A stable bacterial peroxidase with novel halogenating activity and an autocatalytically linked heme prosthetic group.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Auer, Markus Battistuzzi, Gianantonio Furtmüller, Paul G. Kroiss, Daniela Teufer, Stefan A. Obinger, Christian Gruber, Clemens Bellei, Marzia Soudi, Monika Zamocky, Marcel Pirker, Katharina F. Hofbauer, Stefan
Description	Author Affiliation: Auer M ( From the Division of Biochemistry, Department of Chemistry, Vienna Institute of BioTechnology, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria.)
Abstract	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.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	38
Volume Number	288
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2013-09-20
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Bacterial Proteins Chemistry Bromides Cyanobacteria Enzymology Heme Peroxidase Genetics Metabolism Enzyme Stability Physiology Hydrogen-Ion Concentration Oxidation-Reduction Research Support, Non-U.S. Gov't Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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