ArticleThe Journal of biological chemistry2013
A stable bacterial peroxidase with novel halogenating activity and an autocatalytically linked heme prosthetic group.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 20 citations in OpenAlex.
- A Bacterial Myeloperoxidase with Antimicrobial Properties.Biotech (Basel (Switzerland)) · 2023Article
- Secreted heme peroxidase fromThe Journal of biological chemistry · 2018Article
- Pre-steady-state Kinetics Reveal the Substrate Specificity and Mechanism of Halide Oxidation of Truncated Human Peroxidasin 1.The Journal of biological chemistry · 2017Article
- Hydrogen peroxide-mediated conversion of coproheme to heme b by HemQ-lessons from the first crystal structure and kinetic studies.The FEBS journal · 2016Article
- From chlorite dismutase towards HemQ - the role of the proximal H-bonding network in haeme binding.Bioscience reports · 2016Article
- Design, challenge, and promise of stimuli-responsive nanoantibiotics.Nano convergence · 2016Review
- Dimeric chlorite dismutase from the nitrogen-fixing cyanobacterium Cyanothece sp. PCC7425.Molecular microbiology · 2015Article
- Independent evolution of four heme peroxidase superfamilies.Archives of biochemistry and biophysics · 2015Article
- Multidomain human peroxidasin 1 is a highly glycosylated and stable homotrimeric high spin ferric peroxidase.The Journal of biological chemistry · 2015Article
- How covalent heme to protein bonds influence the formation and reactivity of redox intermediates of a bacterial peroxidase.The Journal of biological chemistry · 2014Article
- Heterologous expression and characterization of the manganese-oxidizing protein from Erythrobacter sp. strain SD21.Applied and environmental microbiology · 2014Article
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Authors and funding
12 authors at 2 institutions in 3 countries.
Funding
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.