title: A stable bacterial peroxidase with novel halogenating activity and an autocatalytically linked heme prosthetic group.
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.
authors.affiliation: Division of Biochemistry, Department of Chemistry, Vienna Institute of BioTechnology, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria.
authors.forename: Markus
authors.initials: M
authors.lastname: Auer
authors.affiliation: Division of Biochemistry, Department of Chemistry, Vienna Institute of BioTechnology, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria.
authors.forename: Clemens
authors.initials: C
authors.lastname: Gruber
authors.affiliation: Departments of Life Sciences.
authors.forename: Marzia
authors.initials: M
authors.lastname: Bellei
authors.affiliation: Division of Biochemistry, Department of Chemistry, Vienna Institute of BioTechnology, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria.
authors.forename: Katharina F
authors.initials: KF
authors.lastname: Pirker
authors.affiliation: Division of Biochemistry, Department of Chemistry, Vienna Institute of BioTechnology, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria; Institute of Molecular Biology, Slovak Academy of Sciences, 84551 Bratislava, Slovakia.
authors.forename: Marcel
authors.initials: M
authors.lastname: Zamocky
authors.affiliation: Division of Biochemistry, Department of Chemistry, Vienna Institute of BioTechnology, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria.
authors.forename: Daniela
authors.initials: D
authors.lastname: Kroiss
authors.affiliation: Division of Biochemistry, Department of Chemistry, Vienna Institute of BioTechnology, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria.
authors.forename: Stefan A
authors.initials: SA
authors.lastname: Teufer
authors.affiliation: Division of Biochemistry, Department of Chemistry, Vienna Institute of BioTechnology, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria.
authors.forename: Stefan
authors.initials: S
authors.lastname: Hofbauer
authors.affiliation: Division of Biochemistry, Department of Chemistry, Vienna Institute of BioTechnology, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria.
authors.forename: Monika
authors.initials: M
authors.lastname: Soudi
authors.affiliation: Departments of Chemistry and Geology, University of Modena and Reggio Emilia, 41100 Modena, Italy.
authors.forename: Gianantonio
authors.initials: G
authors.lastname: Battistuzzi
authors.affiliation: Division of Biochemistry, Department of Chemistry, Vienna Institute of BioTechnology, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria.
authors.forename: Paul G
authors.initials: PG
authors.lastname: Furtmüller
authors.affiliation: Division of Biochemistry, Department of Chemistry, Vienna Institute of BioTechnology, BOKU-University of Natural Resources and Life Sciences, Muthgasse 18, A-1190 Vienna, Austria. Electronic address: christian.obinger@boku.ac.at.
authors.forename: Christian
authors.initials: C
authors.lastname: Obinger
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D001965:Bromides / Q000737:chemistry* / Q000378:metabolism; D000458:Cyanobacteria / Q000201:enzymology* / Q000235:genetics; D004795:Enzyme Stability / Q000502:physiology; D006418:Heme / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D010084:Oxidation-Reduction; D009195:Peroxidase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
chemical_list: D001426:Bacterial Proteins; D001965:Bromides; D006418:Heme; D009195:Peroxidase
keywords: Cyanobacteria; Enzyme Catalysis; Heme; Innate Immunity; Peroxidase
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