Oxidation of benzo(a)pyrene by extracellular ligninases of Phanerochaete chrysosporium. Veratryl alcohol and stability of ligninase.

Haemmerli, S.; Leisola, Matti; Sanglard, Dominique; Fiechter, Armin

doi:10.1016/s0021-9258(19)62701-8

Cited by 268 publications

(27 citation statements)

References 27 publications

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“…et al, 1986), and haloperoxidase-type oxidations of bromide and iodide (Renganathan et al, 1987). Recently, both lignin peroxidases and whole cultures of P. chrysosporium were shown to oxidize certain polycyclic aromatic hydrocarbons to polycyclic quiñones, which indicates a biodegradative role for these enzymes in at least some of the pollutant oxidations accomplished by Phanerochaete (Haemmerli et al, 1986;Hammel et al, 1986b). We are interested in the possibility that these peroxidases might be involved in the biodegradation of polychlorinated phenols and now report that they catalyze the oxidative 4-dechlorination of these pollutants.…”

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The oxidative 4-dechlorination of polychlorinated phenols is catalyzed by extracellular fungal lignin peroxidases

Hammel¹,

Tardone²

1988

Biochemistry

188

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The extracellular lignin peroxidases (ligninases) of Phanerochaete chrysosporium catalyzed HzOz-dependent spectral changes in several environmentally significant polychlorinated phenols: 2,4-dichloro-, 2,4,5-trichloro-, 2,4,6-trichloro-, and pentachlorophenol. Gas chromatography/mass spectrometry of reduced and acetylated reaction products showed that, in each case, lignin peroxidase catalyzed a 4-dechlorination of the starting phenol to yield a p-benzoquinone. The oxidation of 2,4-dichlorophenol also yielded a dechlorinated coupling dimer, tentatively identified as 2-chloro-6-(2,4-dichlorophenoxy)-p-benzoquinone. Experiments on the stoichiometry of 2,4,6-trichlorophenol oxidation showed that this substrate was quantitatively dechlorinated to give the quinone and inorganic chloride. Hz'*O-labeling experiments on 2,4,6trichlorophenol oxidation demonstrated that water was the source of the new 4-OXO substituent in 2,6-dichloro-p-benzoquinone. Our results indicate a mechanism whereby lignin peroxidase oxidizes a 4-chlorinated phenol to an electrophilic intermediate, perhaps the 4-chlorocyclohexadienone cation. Nucleophilic attack by water and elimination of HCl then ensue at the 4-position, which produces the quinone. Lignin peroxidases have previously been implicated in the degradation by Phanerochaete of several nonphenolic aromatic pollutants [cf. Haemmerli, S. D., Leisola, M. S.

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confidence: 99%

The oxidative 4-dechlorination of polychlorinated phenols is catalyzed by extracellular fungal lignin peroxidases

Hammel¹,

Tardone²

1988

Biochemistry

188

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“…These isozymes catalyze the H 2 O 2 -dependent oxidation of lignin and lignin model compounds by the initial formation of an aryl cation radical with subsequent nonenzymatic reactions yielding a final product (Tien, 1987;Kirk & Farrell, 1987). It has also been found that the degradation of several xenobiotics involves LiP (Barr & Aust, 1994;Mileski et al, 1988;Bumpus & Brock, 1988;Sanglard et al, 1986;Haemmerli et al, 1986;Hammel et al, 1986Hammel et al, , 1988Schremer et al, 1988). Additionally, many compounds oxidized by LiP have high redox potentials, beyond the reach of plant peroxidases (Gold et al, 1989;Kirk & Farrell, 1987).…”

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Spectral Changes of Lignin Peroxidase during Reversible Inactivation

Nie

Aust

1997

Biochemistry

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The heme environment of lignin peroxidase (LiP) has been investigated by electronic absorption and electron paramagnetic resonance (EPR) spectroscopy. Native LiP was a pentacoordinate, high-spin ferric iron with a high-spin absorption band at 634 nm and g values at 5.86 and 2.07 in the EPR spectrum. Upon thermal inactivation, calcium ions were released from the enzyme and the Soret absorption decreased and red-shifted about 2 nm, the high-spin absorption band at 634 nm disappeared, and a low-spin absorption band appeared at 532 nm. The EPR spectrum and the temperature dependence of electronic absorption spectra revealed that the heme iron of the thermally inactivated enzyme was a mixture of high- and low-spin states, which was further supported by the changes in the electronic absorption and EPR spectra when cyanide was added to the thermally inactivated enzyme. Addition of various imidazoles or CN- to thermally inactivated enzyme demonstrated that the low-spin heme iron of inactivated enzyme was hexacoordinate with a distal histidine as its sixth ligand, in contrast to the active enzyme, which was pentacoordinate and high-spin. Upon addition of calcium to recover the thermally inactivated LiP, the reactivated enzyme had absorptions at 408, 502, and 634 nm and g values at 5.86 and 2.07 in the EPR spectrum, which demonstrated that the heme iron of the reactivated enzyme was again high-spin and pentacoordinated.

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“…It contains multiple isoenzymes with molecular weights of 37-47 kDa, isoelectric points of 3.2-4.7, optimal enzyme activity temperatures of 35-55 °C, optimal pH values of 2.5-3.0, and oxidation-reduction potentials of 1.2-1.5 [26]. Its catalyzed substrate is non-specific and can oxidatively decompose lignin monomers, dimers and trimers, and aromatic ring polymers in the presence of hydrogen peroxide [27][28][29]. The catalytic cycle of LiP mainly includes three steps.…”

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confidence: 99%

Contribution of Lignin Peroxidase, Manganese Peroxidase, and Laccase in Lignite Degradation by Mixed White-Rot Fungi

Shi

Liu

Chen

et al. 2020

Waste Biomass Valor

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The catalytic depolymerization of biological enzymes during biological liquefaction of coal is very important. In this study, the effects of medium types, lignite addition, and mixed culture on lignin peroxidase (LiP), manganese peroxidase (MnP) and laccase (Lac) secreted by white-rot fungi are investigated. Fifteen strains of white-rot fungi are used for microbial liquefaction of the Zhaotong lignite in Yunnan. The results show that the activities of LiP, MnP, and Lac are highest in the Czapek-Dox medium (DOX), followed by the Sabouraud Maltose Broth (SMB) medium, and are almost zero in the Potato Dextrose Agar (PDA) medium. In the early stage of fungal growth, the medium contains sufficient nutrients, and lignite addition induces an inhibitory effect on extracellular enzyme secretion, whereas in the late growth stage characterized by nutrient deficiency, it exhibits an enhancing effect. For fungi pair combinations, if only single enzyme activity was considered, the positive synergistic effect of Lac in the mixed culture of s.commune and SL203 would be the highest, with the synergistic coefficient of 233.33. While three enzymes were considered, the integrated effects of ZTW07 and SL203 are the highest, with Lac, MnP, and LiP producing synergistic coefficients of 158.795, 1.217, and 1.006, respectively. It can be seen that the mixed culture can greatly improve the enzyme activity of white rot fungi and is one of the effective methods to improve the liquefaction efficiency.

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Oxidation of benzo(a)pyrene by extracellular ligninases of Phanerochaete chrysosporium. Veratryl alcohol and stability of ligninase.

Cited by 268 publications

References 27 publications

The oxidative 4-dechlorination of polychlorinated phenols is catalyzed by extracellular fungal lignin peroxidases

The oxidative 4-dechlorination of polychlorinated phenols is catalyzed by extracellular fungal lignin peroxidases

Spectral Changes of Lignin Peroxidase during Reversible Inactivation

Contribution of Lignin Peroxidase, Manganese Peroxidase, and Laccase in Lignite Degradation by Mixed White-Rot Fungi

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