Oxidative degradation of non‐phenolic lignin during lipid peroxidation by fungal manganese peroxidase

Bao, Wuli; Fukushima, Yaichi; Jensen, K. A.; Moen, Mark A.; Hammel, Kenneth E.

doi:10.1016/0014-5793(94)01146-x

Cited by 197 publications

(101 citation statements)

References 24 publications

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“…Incubation of the protein in 18 O-labeled water did not result in any changes in the low-frequency spectrum, as would be expected for a hydroxo-ligated heme iron. Other peroxidases, such as HRP and turnip peroxidase, also exhibit HS f LS transitions at high pH that had been previously attributed to coordination of a distal His to the heme iron (57,58).…”

Section: Discussionsupporting

confidence: 55%

“…Other peroxidases, such as HRP and turnip peroxidase, also exhibit HS f LS transitions at high pH that had been previously attributed to coordination of a distal His to the heme iron (57,58). However, more recent studies have shown that incubation of several HRP isozymes in 18 O-labeled water at high pH results in shifts in the low-frequency RR spectra (50). Bands in the spectra of LS alkaline HRP and turnip peroxidase have since been assigned to Fe-OH stretching at 500-520 cm -1 .…”

Section: Discussionmentioning

confidence: 99%

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Formation of a Bis(histidyl) Heme Iron Complex in Manganese Peroxidase at High pH and Restoration of the Native Enzyme Structure by Calcium

et al. 2000

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Manganese peroxidase (MnP) from Phanerochaete chrysosporium undergoes a pH-dependent conformational change evidenced by changes in the electronic absorption spectrum. This high-to lowspin alkaline transition occurs at ∼2 pH units lower in an F190I mutant MnP when compared to the wild-type enzyme. Herein, we provide evidence that these spectral changes are attributable to the formation of a bis(histidyl) heme iron complex in both proteins at high pH. The resonance Raman (RR) spectra of both ferric proteins at high pH are similar, indicating similar heme environments in both proteins, and resemble that of ferric cytochrome b 558 , a protein that contains a bis-His iron complex. Upon reduction with dithionite at high pH, the visible spectra of both the wild-type and F190I MnP exhibit absorption maxima at 429, 529, and 558 nm, resembling the absorption spectrum of ferrous cytochrome b 558 . RR spectra of the reduced wild-type and F190I mutant proteins at high pH are also similar to the RR spectrum of ferrous cytochrome b 558 , further suggesting that the alkaline low-spin species is a bis(histidyl) heme derivative. No shift in the low-frequency RR bands was observed in 75% 18 O-labeled water, indicating that the low-spin species is most likely not a hydroxo-heme derivative. Electronic and RR spectra also indicate that addition of Ca 2+ to either the ferric or ferrous enzymes at high pH completely restores the high-spin pentacoordinate species. Other divalent metals, such as Mn 2+ , Mg 2+ , Zn 2+ , or Cd 2+ , do not restore the enzyme under the conditions studied.Manganese peroxidase (MnP) 1 is an extracellular heme protein produced by virtually all lignin-degrading white-rot fungi (1-3). Sequences have been determined for mnp cDNA (4, 5) and genomic clones (6-8) encoding three MnP isozymes from Phanerochaete chrysosporium, the beststudied lignin-degrading fungus. These sequences and spectroscopic studies of the native and oxidized enzyme intermediates indicate that the heme environment of MnP is similar to that of other plant and fungal peroxidases (4,(9)(10)(11)(12)(13)(14). Kinetic and spectroscopic studies of the purified enzyme indicate a typical peroxidase reaction catalytic cycle:However, MnP is unique in its ability to efficiently oxidize Mn 2+ to Mn 3+ (9,15,16). The released Mn 3+ is stabilized by organic acid chelators, such as oxalate and malonate, which are secreted by the fungus (16, 17). The Mn 3+ -chelator complex is capable of diffusing from the enzyme to oxidize terminal substrates including lignin substructures, phenolic compounds, and pollutants (2, 3 and references therein, 18).The three amino acid residues believed to bind Mn 2+ , D179, E35, and E39, were investigated by site-directed mutagenesis of recombinant MnP homologously expressed in P. chrysosporium (19)(20)(21)(22). These studies, combined with X-ray crystal structure analyses of the proteins (23,24), confirmed that the side-chain carboxylates of D179, E35, and E39 form the only apparent Mn 2+ -binding site in MnP from P. chry...

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Section: Discussionsupporting

confidence: 55%

Section: Discussionmentioning

confidence: 99%

Formation of a Bis(histidyl) Heme Iron Complex in Manganese Peroxidase at High pH and Restoration of the Native Enzyme Structure by Calcium

et al. 2000

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“…Mn 3+ is efficiently stabilized in aqueous solution by α-hydroxy acids (11). These complexes function as diffusible oxidants that can oxidize terminal phenolic substrates and also possibly nonphenolic substitutents via a radical mediator (3). Lignin peroxidase (LiP) plays a central role in the biodegradation of the plant cell wall constituent lignin.…”

Section: Co2mentioning

confidence: 99%

Screening for ligninolytic enzymes from autochthonous fungi and applications for decolorization of Remazole Marine Blue

Erden¹,

Ucar²,

Gezer³

et al. 2009

Braz. J. Microbiol.

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This study presents new and alternative fungal strains for the production of ligninolytic enzymes which have great potential to use in industrial and biotechnological processes. Thirty autochthonous fungal strains were harvested from Bornova-Izmir in Turkiye. In the fresh fruitbody extracts laccase, manganese peroxidase and lignin peroxidase activities, which are the principal enzymes responsible for ligninocellulose degradation by Basidiomycetes, were screened. Spores of some of the basidiomycetes species such as Cortinarius sp., Trametes versicolor, Pleurotus ostreatus, Abortiporus biennis, Lyophyllum subglobisporium, Ramaria stricta, Ganoderma carnosum, Lactarius delicious ve Lepista nuda were isolated and investigated optimum cultivation conditions in submerged fermentation for high yields of ligninolytic enzyme production. In addition, isolated fungal strains were monitored on agar plates whether having the capability of decolorization of a textile dye Remazol Marine Blue.

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“…They are the heme containing peroxidases, lignin peroxidase (Lip) and manganesedependent peroxidase (Mn P) as well as the copper-containing phenol oxidase, laccase. In the presence of H 2 O 2 , MnP oxidizes Mn 2+ to Mn 3+ , which can oxidize phenolic units in lignin (Bao et al, 1994). One of the most studied applications in the industry is the laccases-mediator bleaching of kraft pulp and the efficiency of which has been proven in mill-scale trials (Strebotnik and Hammel, 2000).Lignin peroxidases (LiP) compared with laccase, are the biocatalysts of choice for bleaching (Bajpai, 2004;Sigoillot et al, 2005) Roy and Archibald (1993) concluded that T. versicolor produces MnP which is important in delignification and bleaching of kraft pulp.…”

Section: Issn: 2319-7706 Volume 6 Number 11 (2017) Pp 2873-2879mentioning

confidence: 99%

Fungal Enzymes in Decolorizing Paper Pulp

Devakumari¹

2017

Int.J.Curr.Microbiol.App.Sci

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Oxidative degradation of non‐phenolic lignin during lipid peroxidation by fungal manganese peroxidase

Cited by 197 publications

References 24 publications

Formation of a Bis(histidyl) Heme Iron Complex in Manganese Peroxidase at High pH and Restoration of the Native Enzyme Structure by Calcium

Formation of a Bis(histidyl) Heme Iron Complex in Manganese Peroxidase at High pH and Restoration of the Native Enzyme Structure by Calcium

Screening for ligninolytic enzymes from autochthonous fungi and applications for decolorization of Remazole Marine Blue

Fungal Enzymes in Decolorizing Paper Pulp

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