Degradation of 2,7-dichlorodibenzo-p-dioxin by the lignin-degrading basidiomycete Phanerochaete chrysosporium

Valli, Khadar; Wariishi, Hiroyuki; Gold, Michael H.

doi:10.1128/jb.174.7.2131-2137.1992

Cited by 227 publications

(164 citation statements)

References 54 publications

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“…Many low molecular weight compounds have been identified which could play a fundamental role in the enzymatic ligninolytic systems of white-rot fungi [104,[107][108][109][110][111]. Lip and MnP can oxidise various lignin compounds and synthetic lignin only in the presence of a cofactor [112][113][114].…”

Section: Low Molecular Weight Compounds Involved In Lignin Degradationmentioning

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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Section: Low Molecular Weight Compounds Involved In Lignin Degradationmentioning

confidence: 99%

Enzymatic Degradation of Lignin in Soil: A Review

et al. 2017

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“…Enzyme-generated Mn III is stabilized by dicarboxylic organic acid chelators, such as oxalate (15,25,26 10.1021/bi002104s CCC: $20.00 © xxxx American Chemical Societyenough to diffuse from the enzyme and oxidize terminal phenolic substrates, including lignin (27) and aromatic pollutants (28)(29)(30)(31). Oxidation of nonphenolic lignin substructures by MnP has been proposed to occur via radical mediators (32,33).…”

mentioning

confidence: 99%

The Role of Glu39 in Mn^II Binding and Oxidation by Manganese Peroxidase from Phanerochaete chrysoporium

Youngs

Gelpke

et al. 2001

Biochemistry

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Manganese peroxidase (MnP) is a heme-containing enzyme produced by white-rot fungi and is part of the extracellular lignin degrading system in these organisms. MnP is unique among Mn binding enzymes in its ability to bind and oxidize Mn II and efficiently release Mn III . Initial site-directed mutagenesis studies identified the residues E35, E39, and D179 as the Mn binding ligands. However, an E39D variant was recently reported to display wild-type Mn binding and rate of oxidation, calling into question the role of E39 as an Mn ligand. To investigate this hypothesis, we performed computer modeling studies which indicated metal-ligand bond distances in the E39D variant and in an E35D-E39D-D179E triple variant which might allow Mn binding and oxidation. To test the model, we reconstructed the E35D and E39D variants used in the previous study, as well as an E39A single variant and the E35D-E39D-D179E triple variant of MnP isozyme 1 from Phanerochaete chrysosporium. We find that all of the variant proteins are impaired for Mn II binding (K m increases 20-30-fold) and Mn II oxidation (k cat decreases 50-400-fold) in both the steady state and the transient state. In particular, mutation of the E39 residue in MnP decreases both Mn binding and oxidation. The catalytic efficiency of the E39A variants decreased ∼10 4 -fold, while that of the E39D variant decreased ∼10 3 -fold. Contrary to initial modeling results, the triple variant performed only as well as any of the single Mn ligand variants. Interestingly, the catalytic efficiency of the triple variant decreased only 10 4 -fold, which is ∼10 2 -fold better than that reported for the E35Q-D179N double variant. These combined studies indicate that precise geometry of the Mn ligands within the Mn binding site of MnP is essential for the efficient binding, oxidation, and release of Mn by this enzyme. The results clearly indicate that E39 is a Mn ligand and that mutation of this ligand decreases both Mn binding and the rate of Mn oxidation.

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“…The biomass accumulation levelled off around day 15 coinciding with the decrease in the MnP activity observed on day 18 in all but the 0 mg control. Studies done in the last 10 years indicated that white rot fungi have the potential to biodegrade the highly toxic PCB and PCB-like (furans and dioxins) group Valli et al, 1992). These studies concentrated on P. chrysosporium as a model organism and lignin peroxidase as model enzyme.…”

Section: Aroclor Biodegradationmentioning

confidence: 99%

Removal of Aroclor 1254 by the white rot fungus Coriolus versicolor in the presence of different concentrations of Mn(IV)oxide

Cloete

Celliers

1999

International Biodeterioration & Biodegradation

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Degradation of 2,7-dichlorodibenzo-p-dioxin by the lignin-degrading basidiomycete Phanerochaete chrysosporium

Cited by 227 publications

References 54 publications

Enzymatic Degradation of Lignin in Soil: A Review

Enzymatic Degradation of Lignin in Soil: A Review

The Role of Glu39 in Mn^II Binding and Oxidation by Manganese Peroxidase from Phanerochaete chrysoporium

Removal of Aroclor 1254 by the white rot fungus Coriolus versicolor in the presence of different concentrations of Mn(IV)oxide

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Degradation of 2,7-dichlorodibenzo-p-dioxin by the lignin-degrading basidiomycete Phanerochaete chrysosporium

Cited by 227 publications

References 54 publications

Enzymatic Degradation of Lignin in Soil: A Review

Enzymatic Degradation of Lignin in Soil: A Review

The Role of Glu39 in MnII Binding and Oxidation by Manganese Peroxidase from Phanerochaete chrysoporium

Removal of Aroclor 1254 by the white rot fungus Coriolus versicolor in the presence of different concentrations of Mn(IV)oxide

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The Role of Glu39 in Mn^II Binding and Oxidation by Manganese Peroxidase from Phanerochaete chrysoporium