Polymerisation of lignins by ligninases from<i>Phanerochaete chrysosporium</i>

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

doi:10.1111/j.1574-6968.1986.tb01494.x

Cited by 154 publications

(52 citation statements)

References 22 publications

(15 reference statements)

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“…Lignin peroxidase was isolated and purified from carbon-limited cultures of P. chrysosporium (ATCC 24725) as described in [7]. The enzyme with ~14.15 was used in all experiments.…”

Section: Enzyme Preparationsmentioning

confidence: 99%

Oxidation of veratryl alcohol by the lignin peroxidase of Phanerochaete chrysosporium Involvement of activated oxygen

Haemmerli¹,

Schoemaker

Schmidt

et al. 1987

FEBS Letters

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The oxidation of veratryl alcohol by the lignin peroxidase of Phanerochaete chrysosporium was studied. Five products were identified: veratraldehyde, two quinones and two aromatic ring cleavage lactones. A similar product pattern was obtained with the 1‐electron oxidant cerium(IV). Under anaerobic reaction conditions or in the presence of Mn(II) only traces of quinones or lactones were detected besides veratraldehyde. This indicates the involvement of activated oxygen species in the enzyme reaction. Possible mechanisms for the formation of the primary oxidation products from veratryl alcohol are discussed.

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“…Lignin peroxidase was isolated and purified from carbon-limited cultures of P. chrysosporium (ATCC 24725) as described in [7]. The enzyme with ~14.15 was used in all experiments.…”

Section: Enzyme Preparationsmentioning

confidence: 99%

Oxidation of veratryl alcohol by the lignin peroxidase of Phanerochaete chrysosporium Involvement of activated oxygen

Haemmerli¹,

Schoemaker

Schmidt

et al. 1987

FEBS Letters

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“…A key component of the fungal ligninolytic system is thought to consist of extracellular lignin peroxidases (LiPs), which catalyze the one-electron oxidation of various lignin-related substrates (6)(7)(8). LiPs have also been shown to oxidize certain PAHs in vitro, and it has been proposed that they play an important role in the degradation of these pollutants by white-rot fungi (9,10). However, it has never been demonstrated that LiP-catalyzed oxidation is a significant fate ofany PAH in vivo or that the products of such a reaction are subsequently cleaved to smaller, monocyclic, compounds.…”

mentioning

confidence: 99%

Ring fission of anthracene by a eukaryote.

Hammel

Green

Gai

1991

Proc. Natl. Acad. Sci. U.S.A.

116

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Ligninolytic fungi are unique among eukaryotes in their ability to degrade polycyclic aromatic hydrocarbons (PAHs), but the mechanism for this process is unknown. Although certain PAHs are oxidized in vitro by the fungal lignin peroxidases (LiPs) that catalyze lig olysis, it has never been shown that LiPs initiate PAH degradation in vivo. To address these problems, the metabolism of anthracene (AC) and its in vitro oxidation product, 9,10-anthraquinone (AQ), was examined by chromatographic and isotope dilution techniques in Phanerochaete chrysosporium. The fungal oxidation of AC to AQ was rapid, and both AC and AQ were significantly mineralized. Both compounds were cleaved by the fungus to give the same ring-flssion metabolite, phthalic acid, and phthalate production from AQ was shown to occur only under ligninolytic culture conditions. These results show that the major pathway for AC degradation in Phanerochaete proceeds AC -+ AQ --phthalate + CO2 and that it is probably mediated by LiPs and other enzymes of ligninolytic metabolism.Polycyclic aromatic hydrocarbons (PAHs) are major pollutants of both anthropogenic and natural pyrolytic origin, occurring in soils, sediments, and airborne particulates. The crucial step in their biodegradation is oxidative fission of the fused aromatic ring system, an event previously thought unique to certain bacteria (1). Recent evidence necessitates a revision of this view: the lignin-degrading fungi that cause white-rot of wood have also been shown to mineralize a wide variety of aromatic pollutants, including certain PAHs, under culture conditions that promote the expression of ligninolytic metabolism (2-5). A key component of the fungal ligninolytic system is thought to consist of extracellular lignin peroxidases (LiPs), which catalyze the one-electron oxidation of various lignin-related substrates (6-8). LiPs have also been shown to oxidize certain PAHs in vitro, and it has been proposed that they play an important role in the degradation of these pollutants by white-rot fungi (9, 10). However, it has never been demonstrated that LiP-catalyzed oxidation is a significant fate ofany PAH in vivo or that the products of such a reaction are subsequently cleaved to smaller, monocyclic, compounds. In fact, to our knowledge, no PAH ring-fission metabolite other than CO2 has ever been identified in any eukaryote. To address these problems, we have examined the fate of anthracene (AC) in cultures of the ligninolytic basidiomycete Phanerochaete chrysosporium, and we now report that ligninolytic metabolism provides a route for the ring fission of this PAH. AC trans-1,2-dihydrodiol was synthesized from 1,2-dihydroxy-AQ (alizarin) as previously described (12, 13) [ring-'4C]Phthalic acid (12.7 mCi-mmol-1, radiochemical purity >98%) was from Sigma. Unlabeled phthalic acid (99%) and AQ (>98%) were from Kodak. All other reagents were of the highest commercially available quality. MATERIALS AND METHODSTo minimize the artifactual oxidation of AC or its metabolites, all syntheses, cultu...

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“…However, because the enzymatic systems do not depolymerize lignin completely [7], a new hypothesis has recently been put forward, proposing that LiP is not prerequisite for lignin degradation during white-rot wood decay processes [8]. Alternatively, it has been addressed that LiP plays primarily a key role in secondary metabolism of veratryl alcohol which is biosynthesized from L-phenylalanine in white-rot fungi, which might have successfully adapted veratryl alcohol peroxidase (VAP) or LiP to degradation of lignins and xenobiotics during their biochemical evolution [9].…”

Section: Introductionmentioning

confidence: 99%

A novel enzymatic decarboxylation of oxalic acid by the lignin peroxidase system of white‐rot fungus Phanerochaete chrysosporium

Akamatsu

Higuchi

et al. 1990

FEBS Letters

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Oxidation of veratryl alcohol by lignin peroxidase (Lip) was potently inhibited by oxalic acid. The inhibition analysis with Lineweaver-Burk plots clearly showed that the type of inhibition is non-competitive. The enzymatic oxidation of veratryl alcohol in the presence of "C-oxalic acid yielded radioactive carbon dioxide. The results indicate that the apparent inhibition of LiP is caused by reduction of the veratryl alcohol cation radical intermediate back to the substrate level by oxalate, which is concomitantly oxidized to carbon dioxide.

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Polymerisation of lignins by ligninases fromPhanerochaete chrysosporium

Cited by 154 publications

References 22 publications

Oxidation of veratryl alcohol by the lignin peroxidase of Phanerochaete chrysosporium Involvement of activated oxygen

Oxidation of veratryl alcohol by the lignin peroxidase of Phanerochaete chrysosporium Involvement of activated oxygen

Ring fission of anthracene by a eukaryote.

A novel enzymatic decarboxylation of oxalic acid by the lignin peroxidase system of white‐rot fungus Phanerochaete chrysosporium

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