ArticleThe FEBS journal2021
Mutational and structural analysis of an ancestral fungal dye-decolorizing peroxidase.
Article in The FEBS journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 22 citations in OpenAlex.
- Dye-Decolorizing Peroxidase for Lignin Depolymerization: a Comprehensive Review on Enzyme Structural Characteristics, Reaction-Influencing Factors and Efficiency-Enhancing Strategies.Applied biochemistry and biotechnology · 2026Review
- Recombinant DyP peroxidases for green synthesis and characterization of poly(pyrogallol).Scientific reports · 2026Article
- Review
- Unveiling the mechanism of dye-decolorizing peroxidase (DyP): unique anthraquinone-directed catalysis exposes a dual-function peroxidase.Applied and environmental microbiology · 2026Article
- Dye-Decolorizing Peroxidase ofACS omega · 2024Article
- Fungal dye-decolorizing peroxidase diversity: roles in either intra- or extracellular processes.Applied microbiology and biotechnology · 2022Article
- Ancestral sequence reconstruction as a tool to study the evolution of wood decaying fungi.Frontiers in fungal biology · 2022Review
- Toward Microbial Recycling and Upcycling of Plastics: Prospects and Challenges.Frontiers in microbiology · 2022Review
- DyP-Type Peroxidases: Recent Advances and Perspectives.International journal of molecular sciences · 2021Review
- Characterization of a Dye-Decolorizing Peroxidase fromJournal of fungi (Basel, Switzerland) · 2021Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Dye-decolorizing peroxidases (DyPs) constitute a superfamily of heme-containing peroxidases that are related neither to animal nor to plant peroxidase families. These are divided into four classes (types A, B, C, and D) based on sequence features. The active site of DyPs contains two highly conserved distal ligands, an aspartate and an arginine, the roles of which are still controversial. These ligands have mainly been studied in class A-C bacterial DyPs, largely because no effective recombinant expression systems have been developed for the fungal (D-type) DyPs. In this work, we employ ancestral sequence reconstruction (ASR) to resurrect a D-type DyP ancestor, AncDyPD-b1. Expression of AncDyPD-b1 in Escherichia coli results in large amounts of a heme-containing soluble protein and allows for the first mutagenesis study on the two distal ligands of a fungal DyP. UV-Vis and resonance Raman (RR) spectroscopic analyses, in combination with steady-state kinetics and the crystal structure, reveal fine pH-dependent details about the heme active site structure and show that both the aspartate (D222) and the arginine (R390) are crucial for hydrogen peroxide reduction. Moreover, the data indicate that these two residues play important but mechanistically different roles on the intraprotein long-range electron transfer process. DATABASE: Structural data are available in the PDB database under the accession number 7ANV.
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