ArticleThe Journal of biological chemistry2014
How covalent heme to protein bonds influence the formation and reactivity of redox intermediates of a bacterial peroxidase.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 16 citations in OpenAlex.
- A Bacterial Myeloperoxidase with Antimicrobial Properties.Biotech (Basel (Switzerland)) · 2023Article
- Naturally Occurring I81N Mutation in Human CytochromeACS omega · 2022Article
- Noncovalent interactions dominate dynamic heme distortion in cytochrome P450 4B1.The Journal of biological chemistry · 2018Article
- 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
- Independent evolution of four heme peroxidase superfamilies.Archives of biochemistry and biophysics · 2015Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The most striking feature of mammalian peroxidases, including myeloperoxidase and lactoperoxidase (LPO) is the existence of covalent bonds between the prosthetic group and the protein, which has a strong impact on their (electronic) structure and biophysical and chemical properties. Recently, a novel bacterial heme peroxidase with high structural and functional similarities to LPO was described. Being released from Escherichia coli, it contains mainly heme b, which can be autocatalytically modified and covalently bound to the protein by incubation with hydrogen peroxide. In the present study, we investigated the reactivity of these two forms in their ferric, compound I and compound II state in a multi-mixing stopped-flow study. Upon heme modification, the reactions between the ferric proteins with cyanide or H2O2 were accelerated. Moreover, apparent bimolecular rate constants of the reaction of compound I with iodide, thiocyanate, bromide, and tyrosine increased significantly and became similar to LPO. Kinetic data are discussed and compared with known structure-function relationships of the mammalian peroxidases LPO and myeloperoxidase.
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Registered trials
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