ArticleArchives of biochemistry and biophysics2015
Independent evolution of four heme peroxidase superfamilies.
Article in Archives of biochemistry and biophysics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.
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91 citing papers in PubMed, 237 citations in OpenAlex.
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- Myeloperoxidase as a therapeutic target for oxidative damage in Alzheimer's disease.Journal of enzyme inhibition and medicinal chemistry · 2025Review
- Deciphering the role of the distal pocket in Staphylococcus aureus coproheme decarboxylase.Journal of inorganic biochemistry · 2025Article
- The chlorite adduct of aquacobalamin: contrast with chlorite dismutase.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2025Article
- Biochemical and Structural Characterisation of a Bacterial Lactoperoxidase.Chembiochem : a European journal of chemical biology · 2025Article
- Characterization of theInternational journal of molecular sciences · 2024Article
- Biomimetic synergistic effect of redox site and Lewis acid for construction of efficient artificial enzyme.Nature communications · 2024Article
- Structure-function characterization of two enzymes from novel subfamilies of manganese peroxidases secreted by the lignocellulose-degrading Agaricales fungi Agrocybe pediades and Cyathus striatus.Biotechnology for biofuels and bioproducts · 2024Article
- Lactoperoxidase catalytically oxidize hydrogen sulfide via intermediate formation of sulfheme derivatives.Redox biochemistry and chemistry · 2024Article
- Characterization ofApplied and environmental microbiology · 2024Article
- Bacterial transformation of lignin: key enzymes and high-value products.Biotechnology for biofuels and bioproducts · 2024Review
- The Structural Biology of Catalase Evolution.Sub-cellular biochemistry · 2024Review
- Mechanism of peroxidasin inactivation in hyperglycemia: Heme damage by reactive oxygen species.Biochemical and biophysical research communications · 2023Article
- Peroxidasin Inhibition by Phloroglucinol and Other Peroxidase Inhibitors.Antioxidants (Basel, Switzerland) · 2023Article
- Identification of Incomplete Annotations of Biosynthesis Pathways in Rhodophytes Using a Multi-Omics Approach.Marine drugs · 2023Article
- Posttranslational modification and heme cavity architecture of human eosinophil peroxidase-insights from first crystal structure and biochemical characterization.The Journal of biological chemistry · 2023Article
- Identification and characterization of two salmon louse heme peroxidases and their potential as vaccine antigens.iScience · 2023Article
- Peroxidase activity of rice (Oryza sativa) hemoglobin: distinct role of tyrosines 112 and 151.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2023Article
31 more citing papers are in PubMed but not listed here.
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Authors and funding
9 authors at 1 institution in 2 countries.
Funding
Abstract
Four heme peroxidase superfamilies (peroxidase-catalase, peroxidase-cyclooxygenase, peroxidase-chlorite dismutase and peroxidase-peroxygenase superfamily) arose independently during evolution, which differ in overall fold, active site architecture and enzymatic activities. The redox cofactor is heme b or posttranslationally modified heme that is ligated by either histidine or cysteine. Heme peroxidases are found in all kingdoms of life and typically catalyze the one- and two-electron oxidation of a myriad of organic and inorganic substrates. In addition to this peroxidatic activity distinct (sub)families show pronounced catalase, cyclooxygenase, chlorite dismutase or peroxygenase activities. Here we describe the phylogeny of these four superfamilies and present the most important sequence signatures and active site architectures. The classification of families is described as well as important turning points in evolution. We show that at least three heme peroxidase superfamilies have ancient prokaryotic roots with several alternative ways of divergent evolution. In later evolutionary steps, they almost always produced highly evolved and specialized clades of peroxidases in eukaryotic kingdoms with a significant portion of such genes involved in coding various fusion proteins with novel physiological functions.
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