Binding and Catalytic Mechanisms of Veratryl Alcohol Oxidation by Lignin Peroxidase: A Theoretical and Experimental Study

Romero, Juan Fernando Cano; Fernández‐Fueyo, Elena; Ávila-Salas, Fabián; Recabarren, Rodrigo; Alzate‐Morales, Jans; Martı́nez, Ángel T.

doi:10.1016/j.csbj.2019.07.002

Cited by 28 publications

(18 citation statements)

References 48 publications

(58 reference statements)

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“…In the case of AauDyPI, a surface tyrosine and tryptophan-based radical centre were reported [63]. Our result is in line with the previously reported LRET pathways in lignin peroxidase (LiP) and versatile peroxidases (VP) [66][67][68]. Using QM/MM approaches and mutagenesis experiments, the authors reported a possible LRET pathway from the substrate to the heme centre involving electron transfer via 3 aromatic amino acids [67].…”

Section: Oxidation Of An ß-Aryl Ether Lignin Model Substrate and Veratryl Alcoholsupporting

confidence: 90%

Structural and Biochemical Characterization of a Dye Decolorizing Peroxidase from <em>Dictyostelium discoideum</em>

Rai

Klare

Reinke

et al. 2021

Preprint

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A novel cytoplasmic dye decolorizing peroxidase from Dictyostelium discoideum was investigated that oxidizes anthraquinone dyes, lignin model compounds and general peroxidase substrates like ABTS efficiently. Unlike related enzymes, an aspartate residue replaces the first glycine of the conserved GXXDG motif in Dictyostelium DyPA. In solution, Dictyostelium DyPA exists as a stable dimer with the side chain of Asp146 contributing to the stabilization of the dimer interface by extending the hydrogen bond network connecting two monomers. To gain mechanistic insights, we solved the Dictyostelium DyPA structures in the absence of substrate as well as in the presence of potassium cyanide and veratryl alcohol to 1.7, 1.85, and 1.6 Å resolution, respectively. The active site of Dictyostelium DyPA has a hexa-coordinated heme iron with a histidine residue at the proximal axial position and either an activated oxygen or CN- molecule at the distal axial position. Asp149 is in an optimal conformation to accept a proton from H2O2 during the formation of compound I. Two potential distal solvent channels and a conserved shallow pocket leading to the heme molecule were found in Dictyostelium DyPA. Further, we identified two substrate-binding pockets per monomer in Dictyostelium DyPA at the dimer interface. Long-range electron transfer pathways associated with a hydrogen-bonding network that connects the substrate-binding sites with the heme moiety are described.

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Section: Oxidation Of An ß-Aryl Ether Lignin Model Substrate and Veratryl Alcoholsupporting

confidence: 90%

Structural and Biochemical Characterization of a Dye Decolorizing Peroxidase from <em>Dictyostelium discoideum</em>

Rai

Klare

Reinke

et al. 2021

Preprint

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“…Interestingly, St DyP exhibited Mn 2+ -oxidizing activity, which was thought to be the catalytic feature of manganese peroxidase and versatile peroxidase [ 27 , 28 ]. Moreover, St DyP was able to oxidize the non-phenolic substrate VA, which is the characteristic of high redox potential peroxidases such as lignin peroxidase and versatile peroxidase [ 29 , 30 ]. These results indicated that St DyP might have great potential for biodegradation due to its catalytic versatility.…”

Section: Resultsmentioning

confidence: 99%

Efficient Degradation of Zearalenone by Dye-Decolorizing Peroxidase from Streptomyces thermocarboxydus Combining Catalytic Properties of Manganese Peroxidase and Laccase

Qin

Xin

et al. 2021

Toxins

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Ligninolytic enzymes, including laccase, manganese peroxidase, and dye-decolorizing peroxidase (DyP), have attracted much attention in the degradation of mycotoxins. Among these enzymes, the possible degradation pathway of mycotoxins catalyzed by DyP is not yet clear. Herein, a DyP-encoding gene, StDyP, from Streptomyces thermocarboxydus 41291 was identified, cloned, and expressed in Escherichia coli BL21/pG-Tf2. The recombinant StDyP was capable of catalyzing the oxidation of the peroxidase substrate 2,2′-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid), phenolic lignin compounds 2,6-dimethylphenol, and guaiacol, non-phenolic lignin compound veratryl alcohol, Mn2+, as well as anthraquinone dye reactive blue 19. Moreover, StDyP was able to slightly degrade zearalenone (ZEN). Most importantly, we found that StDyP combined the catalytic properties of manganese peroxidase and laccase, and could significantly accelerate the enzymatic degradation of ZEN in the presence of their corresponding substrates Mn2+ and 1-hydroxybenzotriazole. Furthermore, the biological toxicities of the main degradation products 15-OH-ZEN and 13-OH-ZEN-quinone might be remarkably removed. These findings suggested that DyP might be a promising candidate for the efficient degradation of mycotoxins in food and feed.

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“…In general, LiP has two calcium‐binding sites that maintain the enzyme's active center and are formed by four disulfide bonds responsible for maintaining the overall structure 33 . Romero et al 85 . described that the oxidation of LiP could happen in the heme cavity typical of peroxidases or when the Trp171 residue is on the enzyme's surface.…”

Section: Wrf and Their Lmesmentioning

confidence: 99%

Lignin‐modifying enzymes: a green and environmental responsive technology for organic compound degradation

Vilar

Bilal

Bharagava

et al. 2021

J of Chemical Tech & Biotech

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The applications of enzymes have reached an increasing prominence in the scenario of biocatalysis, stimulated mainly by advances in biotechnological processes to obtain products of high added value. The justification for this is the relevant growth of industrial activities that promote the production of various organic contaminants. Thus, enzymes offer the potential to improve industrial processes used in the food, pharmaceutical, textile, pulp and paper sectors. Specifically, the lignin‐modifying enzymes (LMEs) produced by white rot fungi are versatile biocatalysts. Due to their high specificity, a higher yield of biotechnological processes can be achieved, allowing one to obtain biodegradable products and reducing the amount of waste generated. Thus, evaluating the ligninolytic capacity of these enzymes can be a practical approach from the point of view of bioremediation to develop sustainable procedures in the treatment of recalcitrant organic compounds. In this context, this review provides an overview of the use of LMEs in industrial applicability, as well as their potential in contaminant degradation. Besides, this approach emerges to elucidate further the mechanisms of action and properties of LMEs, which have been gaining relevance in the context of lignocellulosic biorefinery. © 2021 Society of Chemical Industry (SCI).

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Binding and Catalytic Mechanisms of Veratryl Alcohol Oxidation by Lignin Peroxidase: A Theoretical and Experimental Study

Cited by 28 publications

References 48 publications

Structural and Biochemical Characterization of a Dye Decolorizing Peroxidase from <em>Dictyostelium discoideum</em>

Structural and Biochemical Characterization of a Dye Decolorizing Peroxidase from <em>Dictyostelium discoideum</em>

Efficient Degradation of Zearalenone by Dye-Decolorizing Peroxidase from Streptomyces thermocarboxydus Combining Catalytic Properties of Manganese Peroxidase and Laccase

Lignin‐modifying enzymes: a green and environmental responsive technology for organic compound degradation

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