Molecular Genetics of Lignin-Degrading Fungi and Their Applications in Organopollutant Degradation

Cullen, Daniel

doi:10.1007/978-3-662-03059-2_5

Cited by 4 publications

(4 citation statements)

References 290 publications

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“…Lignin peroxidase (LiP) and manganese peroxidase (MnP) have been the most intensively studied extracellular enzymes of P. chrysosporium, and several reviews summarize their biochemistry (Kirk and Farrell, 1987;Kirk, 1988;Higuchi, 1990;Schoemaker and Leisola, 1990) and genetics (Alic and Gold, 1991;Gold and Alic, 1993;Cullen and Kersten, 1996;Cullen, 1997Cullen, , 2002. These protoporphyrin IX peroxidases are encoded by families of structurally related genes and further modified posttranslationally.…”

Section: Lignin Peroxidases and Manganese-dependent Peroxidasesmentioning

confidence: 99%

“…This review focuses on extracellular oxidative enzymes of P. chrysosporium, with emphasis on recent advances made possible by the genome sequence. Readers are referred to previous reviews for information on the microbiology and physiology of lignocellulose degradation (Kirk and Farrell, 1987;Eriksson et al, 1990;Blanchette, 1991;Kirk and Cullen, 1998) and on the molecular biology of P. chrysosporium (Alic and Gold, 1991;Pease and Tien, 1991;Gold and Alic, 1993;Cullen and Kersten, 1996;Cullen, 1997Cullen, , 2002Cullen and Kersten, 2004;Larrondo et al, 2005b). …”

Section: Introductionmentioning

confidence: 99%

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Extracellular oxidative systems of the lignin-degrading Basidiomycete Phanerochaete chrysosporium

Kersten

Cullen

2007

Fungal Genetics and Biology

302

189

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Section: Lignin Peroxidases and Manganese-dependent Peroxidasesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Extracellular oxidative systems of the lignin-degrading Basidiomycete Phanerochaete chrysosporium

Kersten

Cullen

2007

Fungal Genetics and Biology

302

189

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“…MnP exhibits its lignin depolymerization activity by oxidizing Mn(II) to Mn(III), which then diffuses out of the enzyme to degrade phenolic components of lignin, aided by organic acids secreted by the white rot fungus such as oxalate or malonate. ,,, To demonstrate that our designed MnC c P.1 mutants display a similar activity toward lignin through Mn(III) released from the enzyme, we tested the activity of the triple mutant on a previously reported lignin model compound, guaiacylglycerl-β-guaiacol ether (Figure a), and analyzed the resulting products by HPLC . As with other MnPs, − our mutant was able to degrade guaiacylglycerl-β-guaiacol ether in the presence of Mn(II) (Figure b). We also assessed the activity of the triple mutant on kraft lignin with HPLC using previously reported methods .…”

Section: Resultsmentioning

confidence: 99%

Enhancing Mn(II)-Binding and Manganese Peroxidase Activity in a Designed Cytochrome c Peroxidase through Fine-Tuning Secondary-Sphere Interactions

Hosseinzadeh¹,

Mirts²,

Pfister³

et al. 2016

Biochemistry

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Non-covalent second shell interactions are important in controlling metal-binding affinity and activity in metalloenzymes, but fine-tuning these interactions in designed metalloenzymes has not been fully explored. As a result, most designed metalloenzymes have low metal-binding affinity and activity. Here we identified three mutations in the second coordination shell of an engineered Mn(II)-binding site in cytochrome c peroxidase (called MnCcP.1, containing Glu45, Glu37, and Glu181 ligands) that mimics the native manganese peroxidase (MnP) and explored their effects on both Mn(II)-binding affinity and MnP activity. First, removing a hydrogen bond to Glu45 through Tyr36Phe mutation, enhanced Mn(II)-binding affinity, as evidenced by a decrease of KM of Mn(II) oxidation 2.8 fold. Second, introducing a salt bridge through Lys179Arg improved Glu35 and Glu181 coordination of Mn(II), decreasing KM 2.6 fold. Third, eliminating a steric clash that prevented Glu37 from orienting towards Mn(II) resulted in an 8.6 fold increase in kcat/KM, arising primarily from a 3.6 fold decrease in KM, with a KM value comparable to that of the native enzyme (0.28 mM vs. 0.2 mM for Pleurotus eryngii MnP PS3). We further demonstrated that while the effects of Tyr36Phe and Lys179Arg mutations are additive, other combinations of mutations were antagonistic. Finally, we showed that these MnCcP variants are functional models of MnP that mimic its activity both in Mn(II) oxidation and degradation of a phenolic lignin model compound and kraft lignin. Our results offer molecular insight into the role of non-covalent interactions around metal binding sites for improving metal binding and overall activity; such insight can be applied to rationally enhance these properties in other metalloenzymes and their models.

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“…Lignin is an amorphous and insoluble polymer lacking stereoregularity, which plays a key role in the carbon cycle as the most abundant aromatic compound and as a protective matrix surrounding the cellulose microfibrils of plant cell walls [1] [2]. Fungi collectively referred to as white rot basidiomycetes are the only microbes capable of efficiently depolymerizing and mineralizing this recalcitrant polymer [3] [4]. The most intensively studied white rot fungus, Phanerochaete chrysosporium, secretes an array of peroxidases that act via the generation of aromatic free radicals, which undergo spontaneous cleavage reactions.…”

Section: Introductionmentioning

confidence: 99%

Factors Affecting the Induction of Lignin Peroxidase in Manganese-Deficient Cultures of the White Rot Fungus <i>Phanerochaete chrysosporium</i>

Matityahu¹,

Sitruk²,

Hadar³

et al. 2015

AiM

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The lignin peroxidase (LIP) production and regulation, in manganese ions (Mn 2+ ) deficient cultures of the white rot fungus Phanerochaete chrysosporium, is still not clearly understood. Mn 2+ deficiency is correlated to low levels of manganese containing superoxide dismutase (MnSOD). In this work, we show that despite the low activity level of MnSOD in Mn 2+ -deficient cultures, the presence of H 2 O 2 is essential for the expression of the lip-H2 gene, which encodes for the major LIP isoenzyme produced (LIP-H2). Thus, the H 2 O 2 present in Mn 2+ -deficient cultures is probably produced by other mechanisms rather than dismutation of superoxide ions by MnSOD. Glyoxal oxidase gene (glox) expression was significantly higher than MnSOD (MnSOD1) and cellobiose dehydrogenase (cdh1) expression in Mn 2+ -deficient cultures, indicating its clear involvement in H 2 O 2 production in those cultures. Glyoxal oxidase may compensate the absence of MnSOD activity in Mn 2+ -deficient cultures. The high levels of reactive oxygen species (ROS) needed for the enhancement of LIP expression in Mn2+ -deficient cultures were not directly correlated to the protein kinase C (PKC) activity involved in signal transduction pathway. High level of oxidative stress was observed in MnSOD silenced mutants, grown in the presence of Mn 2+ , indicating that oxidative stress in Mn 2+ -deficient cultures was caused by low levels of MnSOD rather than the deficiency in Mn 2+ . The results of this work can further contribute to the understanding of LIP regulation in Mn 2+ -deficient cultures.

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Molecular Genetics of Lignin-Degrading Fungi and Their Applications in Organopollutant Degradation

Cited by 4 publications

References 290 publications

Extracellular oxidative systems of the lignin-degrading Basidiomycete Phanerochaete chrysosporium

Extracellular oxidative systems of the lignin-degrading Basidiomycete Phanerochaete chrysosporium

Enhancing Mn(II)-Binding and Manganese Peroxidase Activity in a Designed Cytochrome c Peroxidase through Fine-Tuning Secondary-Sphere Interactions

Factors Affecting the Induction of Lignin Peroxidase in Manganese-Deficient Cultures of the White Rot Fungus <i>Phanerochaete chrysosporium</i>

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Molecular Genetics of Lignin-Degrading Fungi and Their Applications in Organopollutant Degradation

Cited by 4 publications

References 290 publications

Extracellular oxidative systems of the lignin-degrading Basidiomycete Phanerochaete chrysosporium

Extracellular oxidative systems of the lignin-degrading Basidiomycete Phanerochaete chrysosporium

Enhancing Mn(II)-Binding and Manganese Peroxidase Activity in a Designed Cytochrome c Peroxidase through Fine-Tuning Secondary-Sphere Interactions

Factors Affecting the Induction of Lignin Peroxidase in Manganese-Deficient Cultures of the White Rot Fungus &lt;i&gt;Phanerochaete chrysosporium&lt;/i&gt;

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Factors Affecting the Induction of Lignin Peroxidase in Manganese-Deficient Cultures of the White Rot Fungus <i>Phanerochaete chrysosporium</i>