Mn(II) oxidation is the principal function of the extracellular Mn-peroxidase from Phanerochaete chrysosporium

Glenn, Jeffrey K.; Akileswaran, Lakshmi; Gold, Michael H.

doi:10.1016/0003-9861(86)90378-4

Cited by 438 publications

(313 citation statements)

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“…Sequences have been determined for mnp cDNA (4,5) and genomic clones (6)(7)(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:…”

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confidence: 62%

“…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).…”

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confidence: 66%

“…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).…”

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

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“…The function of Mn oxidation in fungi is believed to primarily involve the depolymerisation of lignin, using Mn (III) as the final redox mediator in the breakup of randomly assembled, enzyme-resistant polyphenolic structures (Thompson and Huber, 2007). The oxidation of Mn is said to be the sole reaction performed by Mn-peroxidase (Thompson and Huber, 2007) and requires reduced Mn as a cofactor (Glenn et al, 1986). When Mn-peroxidase oxidizes Mn (II) to Mn (III), the Mn (III) complexed to lactate or other alpha-hydroxy acids is able to oxidize all of the compounds which are oxidized by the enzymatic system (Glenn et al, 1986).…”

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confidence: 99%

EFFECT OF MICRONUTRIENTS-ENRICHED FERTILIZERS ON BASAL STEM ROT DISEASE INCIDENCE AND SEVERITY ON OIL PALM (<i>ELAEIS GUINEENSIS</i> JACQ.) SEEDLINGS

Hanafi¹,

Idris²,

Kadir³

et al. 2014

American Journal of Applied Sciences

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“…The relatively stable Mn III -organic acid complex acts as a diffusible mediator to oxidize the terminal phenolic substrate lignin (24)(25)(26). In the absence of Mn II , MnP intermediates can directly oxidize small phenolic substrates, such as guaiacol and dimethoxyphenol, but only at very slow rates, insufficient for enzyme turnover (13,(27)(28)(29). Whether a Mn II -chelator complex binds to the enzyme to form a ternary complex or the chelator simply facilitates release of Mn III via ligand displacement has not been completely resolved.…”

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High-Resolution Crystal Structure of Manganese Peroxidase: Substrate and Inhibitor Complexes^,

et al. 2005

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Manganese peroxidase (MnP) is an extracellular heme enzyme that catalyzes the peroxidedependent oxidation of Mn II to Mn III . The Mn III is released from the enzyme in complex with oxalate. One heme propionate and the side chains of Glu35, Glu39, and Asp179 were identified as Mn II ligands in the 2.0 Å resolution crystal structure. The new 1.45 Å crystal structure of MnP complexed with Mn II provides a more accurate view of the Mn-binding site. New features include possible partial protonation of Glu39 in the Mn-binding site and glycosylation at Ser336. This is also the first report of MnPinhibitor complex structures. At the Mn-binding site, divalent Cd II exhibits octahedral, hexacoordinate ligation geometry similar to that of Mn II . Cd II also binds to a putative second weak metal-binding site with tetrahedral geometry at the C-terminus of the protein. Unlike that for Mn II and Cd II , coordination of trivalent Sm III at the Mn-binding site is octacoordinate. Sm III was removed from a MnP-Sm III crystal by soaking the crystal in oxalate and then reintroduced into the binding site. Thus, direct comparisons of Sm III -bound and metal-free structures were made using the same crystal. No ternary complex was observed upon incubation with oxalate. The reversible binding of Sm III may be a useful model for the reversible binding of Mn III to the enzyme, which is too unstable to allow similar examination.White-rot basidiomycetous fungi are the only organisms capable of degrading the phenylpropanoid, plant cell wall polymer, lignin (1-4). The lignin-degrading system of these fungi also can oxidize a variety of economically and environmentally important aromatic pollutants (5-9). Under ligninolytic conditions, the best-studied lignin-degrading fungus, Phanerochaete chrysosporium, secretes two families of extracellular heme peroxidases, lignin peroxidase (LiP) and manganese peroxidase (MnP) 1 (2-4, 10), and a hydrogen peroxide-generating system (2, 4, 6).MnP from P. chrysosporium has been studied extensively by a variety of biochemical and biophysical methods (11)(12)(13)(14)(15). The crystal structure illustrates that the heme environment of MnP is similar to that of other plant and fungal peroxidases (16). However, MnP is the only heme peroxidase capable of the one-electron oxidation of Mn II in a typical peroxidase reaction cycle:where MnPI and MnPII are the oxidized intermediates MnP compounds I and II, respectively. The 2.0 Å resolution crystal structure of MnP, determined at room temperature, shows that the substrate, Mn II , binds to one heme propionate and the side chains of three amino acids, Glu35, Glu39, and Asp179, as well as two solvent ligands (16) (Figure 1). This site was confirmed by kinetic and biophysical studies of wild-type MnP and of proteins containing point mutations in the putative binding site. † This research was supported by Grants GM42614 (to T.L.P.) and DK62524 (to M.S.) from the National Institutes of Health and Grants MCB-9808420 from the National Science Foundation and DE-03-9...

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Mn(II) oxidation is the principal function of the extracellular Mn-peroxidase from Phanerochaete chrysosporium

Cited by 438 publications

References 33 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

EFFECT OF MICRONUTRIENTS-ENRICHED FERTILIZERS ON BASAL STEM ROT DISEASE INCIDENCE AND SEVERITY ON OIL PALM (<i>ELAEIS GUINEENSIS</i> JACQ.) SEEDLINGS

High-Resolution Crystal Structure of Manganese Peroxidase: Substrate and Inhibitor Complexes^,

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Mn(II) oxidation is the principal function of the extracellular Mn-peroxidase from Phanerochaete chrysosporium

Cited by 438 publications

References 33 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

EFFECT OF MICRONUTRIENTS-ENRICHED FERTILIZERS ON BASAL STEM ROT DISEASE INCIDENCE AND SEVERITY ON OIL PALM (<i>ELAEIS GUINEENSIS</i> JACQ.) SEEDLINGS

High-Resolution Crystal Structure of Manganese Peroxidase: Substrate and Inhibitor Complexes,

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High-Resolution Crystal Structure of Manganese Peroxidase: Substrate and Inhibitor Complexes^,