Versatile Peroxidase Oxidation of High Redox Potential Aromatic Compounds: Site-directed Mutagenesis, Spectroscopic and Crystallographic Investigation of Three Long-range Electron Transfer Pathways

Pérez-Boada, Marta; Ruíz-Dueñas, Francisco J.; Pogni, Rebecca; Basosi, Riccardo; Choinowski, Thomas; Martı́nez, Marı́a Jesús; Piontek, Klaus; Martı́nez, Ángel T.

doi:10.1016/j.jmb.2005.09.047

Cited by 244 publications

(232 citation statements)

References 65 publications

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“…The RB5 binding site with the lowest free energy of binding (Fig. 5) was found to be consistent with the experimental evidence (Perez-Boadal et al 2005). In this binding mode RB5 is stabilized by seven hydrogen bonds (Table 2).…”

Section: Docking Of Reactive Black 5 and Tween 80supporting

confidence: 86%

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Microbial Decolorization of an Azo Dye Reactive Black 5 Using White-Rot Fungus Pleurotus eryngii F032

Hadibarata

Adnan

Yusoff

et al. 2013

Water Air Soil Pollut

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The growth of white-rot fungus Pleurotus eryngii F032 in a suitable medium can degrade an azo dye Reactive Black 5 (RB5), because of its ability to produce ligninolytic enzymes such as lignin peroxidase (LiP), manganese peroxidase (MnP), and laccase that able to degrade and transform the complex structure of the dye into a less toxic compound. The effect of environmental factors such as initial concentration of Reactive Black 5, pH, temperature of growth medium, surfactant (Tween 80), and agitation were also investigated. The productions of ligninolytic enzymes were enhanced by increasing the white-rot fungi growth in optimum conditions. The decolorization of Reactive Black 5 were analyzed by using UV-vis spectrophotometer at the maximum absorbance of 596 nm. The whiterot fungus, P. eryngii F032 culture exhibited 93.56 % decolorization of 10 mg/L RB5 within 72 h of incubation in dark condition with agitation. The optimum pH and temperature for the decolorizing activity was recorded at pH 3 and 40°C, respectively. The addition of surfactant (Tween 80) increased the decolorization to 93.57 % and agitation of growth medium at 120 rpm enhanced the distribution of nutrients to the fungus thus optimized the enzymatic reaction that resulted maximum decolorization of RB5 which was 93.57 %. The molecular docking studies were performed using Chimera visualization software as to analyze the decolorization mechanism of RB5 at molecular level.

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Section: Docking Of Reactive Black 5 and Tween 80supporting

confidence: 86%

“…The RB5 is docked about 4 Å away from Trp 164 (Fig. 6) which accept electron from RB5 and pass the electron on to Leu 165 and finally to heme group (Perez-Boadal et al 2005). Perez-Boadal et al (2005) also showed that Trp 164 is the vital component for the oxidation of RB5.…”

Section: Docking Of Reactive Black 5 and Tween 80mentioning

confidence: 94%

Microbial Decolorization of an Azo Dye Reactive Black 5 Using White-Rot Fungus Pleurotus eryngii F032

Hadibarata

Adnan

Yusoff

et al. 2013

Water Air Soil Pollut

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“…However, unlike MnP, VP has the dual ability to oxidize Mn 2+ in the independent oxidation of simple amines and phenolic monomers [76]. VP can also oxidize a variety of substrates (with high and low redox potentials) including Mn 2+ , phenolic and non-phenolic lignin dimers, and aromatic alcohols [77].…”

Section: Laccase (mentioning

confidence: 99%

Enzymatic Degradation of Lignin in Soil: A Review

et al. 2017

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Lignin is a major component of soil organic matter and also a rich source of carbon dioxide in soils. However, because of its complex structure and recalcitrant nature, lignin degradation is a major challenge. Efforts have been made from time to time to understand the lignin polymeric structure better and develop simpler, economical, and bio-friendly methods of degradation. Certain enzymes from specialized bacteria and fungi have been identified by researchers that can metabolize lignin and enable utilization of lignin-derived carbon sources. In this review, we attempt to provide an overview of the complexity of lignin's polymeric structure, its distribution in forest soils, and its chemical nature. Herein, we focus on lignin biodegradation by various microorganism, fungi and bacteria present in plant biomass and soils that are capable of producing ligninolytic enzymes such as lignin peroxidase (LiP), manganese peroxidase (MnP), versatile peroxidase (VP), and dye-decolorizing peroxidase (DyP). The relevant and recent reports have been included in this review.

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“…By reducing H 2 O 2 , peroxidases obtain a high redox potential and are thereby able to oxidize a wide range of substrates. Lignin degradation by LiP is mediated by the oxidation of aromatic substrates (Pérez-Boada et al, 2005). Manganese peroxidases oxidize Mn(II) to Mn(III), which becomes chelated with oxalic acid or other organic acids.…”

Section: Introductionmentioning

confidence: 99%

ClassII peroxidase-encoding genes are present in a phylogenetically wide range of ectomycorrhizal fungi

Bödeker

Nygren

Taylor³

et al. 2009

The ISME Journal

158

123

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Fungal peroxidases (ClassII) have a key role in degrading recalcitrant polyphenolic compounds in boreal forest wood, litter and humus. To date, their occurrence and activity have mainly been studied in a small number of white-rot wood decomposers. However, peroxidase activity is commonly measured in boreal forest humus and mineral soils, in which ectomycorrhizal fungi predominate. Here, we used degenerate PCR primers to investigate whether peroxidase-encoding genes are present in the genomes of a wide phylogenetic range of ectomycorrhizal taxa. Cloning and sequencing of PCR products showed that ectomycorrhizal fungi from several different genera possess peroxidase genes. The new sequences represent four major homobasidiomycete lineages, but the majority is derived from Cortinarius, Russula and Lactarius. These genera are ecologically important, but consist mainly of non-culturable species from which little ecophysiological information is available. The amplified sequences contain conserved active sites, both for folding and substrate oxidation. In some Cortinarius spp., there is evidence for gene duplications during the evolution of the genus. ClassII peroxidases seem to be an ancient and a common feature of most homobasidiomycetes, including ectomycorrhizal fungi. Production of extracellular peroxidases may provide ectomycorrhizal fungi with access to nitrogen sequestered in complex polyphenolic sources.

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Versatile Peroxidase Oxidation of High Redox Potential Aromatic Compounds: Site-directed Mutagenesis, Spectroscopic and Crystallographic Investigation of Three Long-range Electron Transfer Pathways

Cited by 244 publications

References 65 publications

Microbial Decolorization of an Azo Dye Reactive Black 5 Using White-Rot Fungus Pleurotus eryngii F032

Microbial Decolorization of an Azo Dye Reactive Black 5 Using White-Rot Fungus Pleurotus eryngii F032

Enzymatic Degradation of Lignin in Soil: A Review

ClassII peroxidase-encoding genes are present in a phylogenetically wide range of ectomycorrhizal fungi

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