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At least 793 records · Page 44Linked to original sources
PubMed1990

Lignin peroxidase oxidation of Mn2+ in the presence of veratryl alcohol, malonic or oxalic acid, and oxygen.

Veratryl alcohol (3,4-dimethoxybenzyl alcohol) appears to have multiple roles in lignin degradation by Phanerochaete chrysosporium. It is synthesized de novo by the fungus. It apparently induces expression of lignin peroxidase (LiP), and it protects LiP from inactivation by H2O2. In addition, veratryl alcohol has been shown to potentiate LiP oxidation of compounds that are not good LiP substrates. We have now observed the formation of Mn3+ in reaction mixtures containing LiP, Mn2+, veratryl alcohol, malonate buffer, H2O2, and O2. No Mn3+ was formed if veratryl alcohol or H2O2 was omitted. Mn3+ formation also showed an absolute requirement for oxygen, and oxygen consumption was observed in the reactions. This suggests involvement of active oxygen species. In experiments using oxalate (a metabolite of P. chrysosporium) instead of malonate, similar results were obtained. However, in this case, we detected (by ESR spin-trapping) the production of carbon dioxide anion radical (CO2.-) and perhydroxyl radical (.OOH) in reaction mixtures containing LiP, oxalate, veratryl alcohol, H2O2, and O2. Our data indicate the formation of oxalate radical, which decays to CO2 and CO2.-. The latter reacts with O2 to form O2.-, which then oxidizes Mn2+ to Mn3+. No radicals were detected in the absence of veratryl alcohol. These results indicate that LiP can indirectly oxidize Mn2+ and that veratryl alcohol is probably a radical mediator in this system.

Basidiomycota↗
PubMed1996

Stabilization of the veratryl alcohol cation radical by lignin peroxidase.

Lignin peroxidase (LiP) catalyzes the H2O2-dependent oxidation of veratryl alcohol (VA) to veratryl aldehyde, with the enzyme-bound veratryl alcohol cation radical (VA.+) as an intermediate [Khindaria et al. (1995) Biochemistry 34, 16860-16869]. The decay constant we observed for the enzyme generated cation radical did not agree with the decay constant in the literature [Candeias and Harvey (1995) J. Biol. Chem. 270, 16745-16748] for the chemically generated radical. Moreover, we have found that the chemically generated VA.+ formed by oxidation of VA by Ce(IV) decayed rapidly with a first-order mechanism in air- or oxygen-saturated solutions, with a decay constant of 1.2 x 10(3) s-1, and with a second-order mechanism in argon-saturated solution. The first-order decay constant was pH- independent suggesting that the rate-limiting step in the decay was deprotonation. When VA.+ was generated by oxidation with LiP the decay also occurred with a first-order mechanism but was much slower, 1.85 s-1, and was the same in both oxygen- and argon-saturated reaction mixtures. However, when the enzymatic reaction mixture was acid-quenched the decay constant of VA.+ was close to the one obtained in the Ce(IV) oxidation system, 9.7 x 10(2) s-1. This strongly suggested that the LiP-bound VA.+ was stabilized and decayed more slowly than free VA.+. We propose that the stabilization of VA.+ may be due to the acidic microenvironment in the enzyme active site, which prevents deprotonation of the radical and subsequent reaction with oxygen. We have also obtained reversible redox potential of VA.+/VA couple using cyclic voltammetery. Due to the instability of VA.+ in aqueous solution the reversible redox potential was measured in acetone, and was 1.36 V vs normal hydrogen electrode. Our data allow us to propose that enzymatically generated VA.+ can act as a redox mediator but not as a diffusible oxidant for LiP-catalyzed lignin or pollutant degradation.

Basidiomycota↗
PubMedDate not supplied

2,4-Dichlorophenol degradation using Streptomyces viridosporus T7A lignin peroxidase.

The Streptomyces viridosporus T7A bacterium produces the extracellular lignin peroxidase ALiP-P3. The ALiP-P3-catalyzed oxidation of 2,4-dichlorophenol (DCP) was examined to understand its kinetic behavior. Initial rate data of the oxidation of DCP were obtained by a spectrophotometric peroxidase assay, and the kinetics were best modeled with a random-binding bireactant system, which differs from the ping-pong bireactant system that is typically used for horseradish peroxidase and lignin peroxidase from the fungus Phanerochaete chrysosporium, and suggests that either DCP or H2O2 may bind first to ALiP-P3. Chloride ion measurements indicate that 16% of the reacted DCP was fully dechlorinated by ALiP-P3. Chemical ionization mass spectrometry was also utilized to identify the DCP degradation product as a hydrophobic chlorinated dimer of mass 322.

Anions↗
PubMed1999

Photochemical mineralization of synthetic lignin in lake water indicates enhanced turnover of aromatic organic matter under solar radiation

The degradation of 14C-[ring]-labelled synthetic lignin (14C-DHP) and dissolved organic carbon (DOC) from lake water were studied simultaneously. 14C-DHP was incubated in humic lake water (colour 173 mg Pt 1(-1)) for 7 d in the dark or under solar radiation. In the dark <0.4% of the introduced 14C-DHP label and 4% of the indigenous DOC were mineralized, indicating that the 14C-labelled aromatic rings of DHP and the humic DOC were microbiologically recalcitrant. Under solar radiation (116 MJ m(-2)), 17-21% of the 14C-labelled carbons in DHP and 18-23% of the indigenous DOC were mineralized in 7 d. Simultaneously the water solubility of 14C-DHP increased. Solar radiation converted the aromatic cores of synthetic lignin to CO2 and soluble organic photoproducts. The results suggest that solar radiation plays a key role in the decomposition of natural polyaromatic matter.

Journal Article↗
PubMed2004

Catechin and hydroxybenzhydrols as models for the environmental photochemistry of tannins and lignins.

The photochemistry of several model plant-derived compounds has been studied in aqueous solution. In particular, the reactions of catechin as a model tannin and methoxy-substituted hydroxybenzhydrols as model lignin functionalities were investigated. Tannins and lignins constitute a significant portion of the humic substances in aquatic systems, which are themselves the main component of dissolved organic matter thought to be responsible for the absorption and attenuation of light in these environments. Catechin (1) was found to undergo a reversible photoisomerization reaction to give epicatechin (2). Such a reaction is an explicit example of a photon absorbing process that enables catechin (1) and its derivatives to act as natural sunscreens by attenuating light energy through non-destructive reactions. The methoxy-substituted hydroxybenzhydrols were found to undergo photosolvolysis reactions via efficient generation of quinone methide intermediates. The intermediate quinone methides were observed to be longer lived, and thus more stable, than previously studied hydroxybenzhydrol derivatives. The meta-hydroxybenzhydrol isomer (5) was found to undergo additional chemistry leading to the production of a ring-closed fluorene from the quinone methide intermediate.

Journal Article↗
PubMed2003

Oxidation of thioanisole and p-methoxythioanisole by lignin peroxidase: kinetic evidence of a direct reaction between compound II and a radical cation.

The reaction of H2O2 with thioanisole and p-methoxythioanisole catalysed by lignin peroxidase from Phanerochaete chrysosporium has been studied spectrophotometrically under turnover and single turnover conditions with a stopped-flow apparatus. Pre-formed lignin peroxidase compounds I and II are each able to react with the sulphides to form a sulphide radical cation. The radical cation is then converted into the sulphoxide either by reaction with the medium or by reaction with compound II. This is the first report of a direct reaction between compound II and the substrate radical cation. With thioanisole, significant enantiomeric selectivity and high oxygen incorporation in the sulphoxide are obtained because compound II is preferentially reduced by the enzyme-bound thioanisole radical cation compared with the neutral substrate. By contrast, with p-methoxythioanisole, the data imply formation of an intermediate ternary complex comprising compound II, radical cation and neutral substrate, such that a chain of electron transfer reactions starting from neutral molecule and progressing to oxidized haem via substrate radical cation is facilitated, yielding the native enzyme and two molecules of p-methoxythioanisole radical cation as products. The reactions of compounds I and II with sulphides imply flexing of the apoprotein moiety during catalysis.

Cations↗
PubMed1985

Exhaustive laccase-catalysed oxidation of a lignin model compound (vanillyl glycol) produces methanol and polymeric quinoid products.

Laccase-catalysed oxidation of the lignin-related phenol vanillyl glycol results in the initial formation of dimers and subsequent polymerization. The polymerization is accompanied by a liberation of methanol corresponding to 15-20% demethylation. Visible spectra together with reduction experiments suggest the simultaneous formation of o-quinones. The participation of quinone formation in the polymerization process and the possible role of such intermediates in lignin biodegradation is discussed.

Laccase↗
PubMed1999

Oxidative polymerization of ribonuclease A by lignin peroxidase from Phanerochaete chrysosporium. Role of veratryl alcohol in polymer oxidation.

The mechanism of lignin peroxidase (LiP) was examined using bovine pancreatic ribonuclease A (RNase) as a polymeric lignin model substrate. SDS/PAGE analysis demonstrates that an RNase dimer is the major product of the LiP-catalyzed oxidation of this protein. Fluorescence spectroscopy and amino acid analyses indicate that RNase dimer formation is due to the LiP-catalyzed oxidation of Tyr residues to Tyr radicals, followed by intermolecular radical coupling. The LiP-catalyzed polymerization of RNase in strictly dependent on the presence of veratryl alcohol (VA). In the presence of 100 microM H2O2, relatively low concentrations of RNase and VA, together but not individually, can protect LiP from H2O2 inactivation. The presence of RNase strongly inhibits VA oxidation to veratraldehyde by LiP; whereas the presence of VA does not inhibit RNase oxidation by LiP. Stopped-flow and rapid-scan spectroscopy demonstrate that the reduction of LiP compound I (LiPI) to the native enzyme by RNase occurs via two single-electron steps. At pH 3.0, the reduction of LiPI by RNase obeys second-order kinetics with a rate constant of 4.7 x 10(4) M-1.s-1, compared to the second-order VA oxidation rate constant of 3.7 x 10(5) M-1.s-1. The reduction of LiP compound II (LiPII) by RNase also follows second-order kinetics with a rate constant of 1.1 x 10(4) M-1.s-1, compared to the first-order rate constant for LiPII reduction by VA. When the reductions of LiPI and LiPIi are conducted in the presence of both VA and RNase, the rate constants are essentially identical to those obtained with VA alone. These results suggest that VA is oxidized by LiP to its cation radical which, while still in its binding site, oxidizes RNase.

Animals↗
PubMed1992

cAMP-mediated differential regulation of lignin peroxidase and manganese-dependent peroxidase production in the white-rot basidiomycete Phanerochaete chrysosporium.

Lignin peroxidases (LIPs) and manganese-dependent peroxidases (MNPs) are major components of the lignin-degrading enzyme system of Phanerochaete chrysosporium and typically appear during secondary metabolism. The involvement of cAMP in the regulation of production of LIPs and MNPs was investigated in this study. Production of LIPs and MNPs was preceded by a sharp rise in intracellular cAMP concentration. Addition of atropine, theophylline, or histamine to cultures resulted in a drop in intracellular cAMP concentration and a concomitant inhibition of production of LIPs only or of both LIPs and MNPs, depending on the concentration of the inhibitor added. These results were independently confirmed by fast protein liquid chromatographic profiles of the LIPs and MNPs in the extracellular fluid of the inhibitor-treated and untreated control cultures. LIP production was generally more sensitive to the inhibitors than MNP production. Northern blot analyses showed that the inhibitors affect the production of LIPs and MNPs at the level of transcription. Furthermore, LIP and MNP gene expression appears to be differentially regulated depending on the intracellular concentration of cAMP. These results show that cAMP plays a key role in the regulation of production of LIPs and MNPs in P. chrysosporium.

Atropine↗
PubMed1997

Oxidation of 4-methoxymandelic acid by lignin peroxidase. Mediation by veratryl alcohol.

The mechanism of veratryl alcohol-mediated oxidation of 4-methoxymandelic acid by lignin peroxidase was studied by kinetic methods. For monomethoxylated substrates not directly oxidized by lignin peroxidase, veratryl alcohol has been proposed to act as a redox mediator. Our previous study showed that stimulation of anisyl alcohol oxidation by veratryl alcohol was not due to mediation but rather due to the requirement of veratryl alcohol to complete the catalytic cycle. Anisyl alcohol can react with compound I but not with compound II. In contrast, veratryl alcohol readily reduces compound II. We demonstrate in the present report that the oxidation of 4-methoxy mandelic acid is mediated by veratryl alcohol. Increasing veratryl alcohol concentration in the presence of 2 mM 4-methoxymandelic acid resulted in increased oxidation of 4-methoxymandelic acid yielding anisaldehyde. This is in contrast to results obtained with anisyl alcohol where increased concentrations of veratryl alcohol caused a decrease in product formation. ESR spectroscopy demonstrated that 4-methoxymandelic acid caused a decrease in the enzyme-bound veratryl alcohol cation radical signal, which is consistent with its reaction at the active site of the enzyme.

Benzyl Alcohols↗
PubMed2001

Initial steps of ferulic acid polymerization by lignin peroxidase.

The major products of the initial steps of ferulic acid polymerization by lignin peroxidase included three dehydrodimers resulting from beta-5' and beta-beta'coupling and two trimers resulting from the addition of ferulic acid moieties to decarboxylated derivatives of beta-O-4'- and beta-5'-coupled dehydrodimers. This is the first time that trimers have been identified from peroxidase-catalyzed oxidation of ferulic acid, and their formation appears to be favored by decarboxylation of dehydrodimer intermediates. After initial oxidation, the coupling reactions appear to be determined by the chemistry of ferulic acid phenoxy radicals, regardless of the enzyme and of whether the reaction is performed in vitro or in vivo. This claim is supported by our finding that horseradish peroxidase provides a similar product profile. Furthermore, two of the dehydrodimers were the two products obtained from laccase-catalyzed oxidation (Tatsumi, K. S., Freyer, A., Minard, R. D., and Bollag, J.-M. (1994) Environ. Sci. Technol. 28, 210-215), and the most abundant dehydrodimer is the most prominent in grass cell walls (Ralph, J., Quideau, S., Grabber, J. H., and Hatfield, R. D. (1994) J. Chem. Soc. Perkin Trans. 1, 3485-3498). Our results also indicate that the dehydrodimers and trimers are further oxidized by lignin peroxidase, suggesting that they are only intermediates in the polymerization of ferulic acid. The extent of polymerization appears to be dependent on the ionization potential of formed intermediates, H(2)O(2) concentration, and, probably, enzyme stability.

Chromatography, Gel↗
PubMed1998

The AmMYB308 and AmMYB330 transcription factors from antirrhinum regulate phenylpropanoid and lignin biosynthesis in transgenic tobacco

MYB-related transcription factors are known to regulate different branches of flavonoid metabolism in plants and are believed to play wider roles in the regulation of phenylpropanoid metabolism in general. Here, we demonstrate that overexpression of two MYB genes from Antirrhinum represses phenolic acid metabolism and lignin biosynthesis in transgenic tobacco plants. The inhibition of this branch of phenylpropanoid metabolism appears to be specific to AmMYB308 and AmMYB330, suggesting that they recognize their normal target genes in these transgenic plants. Experiments with yeast indicate that AmMYB308 can act as a very weak transcriptional activator so that overexpression may competitively inhibit the activity of stronger activators recognizing the same target motifs. The effects of the transcription factors on inhibition of phenolic acid metabolism resulted in complex modifications of the growth and development of the transgenic plants. The inhibition of monolignol production resulted in plants with at least 17% less lignin in their vascular tissue. This reduction is of importance when designing strategies for the genetic modification of woody crops.

Journal Article↗
PubMed1984

Hydroxyproline-Rich Protein Material in Wood and Lignin of Fagus sylvatica.

The nitrogen content, distribution, and amino acid composition of protein material were determined in wood and lignin of Fagus sylvatica. The data indicated that the nitrogen originated from hydroxyproline-rich cell wall glycoprotein, about half of which may be bound to the lignin polymer. The implications for lignocellulose biodegradation are discussed.

Journal Article↗
PubMed1985

Aromatic and Volatile Acid Intermediates Observed during Anaerobic Metabolism of Lignin-Derived Oligomers.

Anaerobic enrichment cultures acclimated for 2 years to use a C-labeled, lignin-derived substrate with a molecular weight of 600 as a sole source of carbon were characterized by capillary and packed column gas chromatography. After acclimation, several of the active methanogenic consortia were inhibited with 2-bromoethanesulfonic acid, which suppressed methane formation and enhanced accumulation of a series of metabolic intermediates. Volatile fatty acids levels in 2-bromoethanesulfonic acid-amended cultures were 10 times greater than those in the uninhibited, methane-forming consortia with acetate as the predominant component. Furthermore, in the 2-bromoethanesulfonic acid-amended consortia, almost half of the original substrate carbon was metabolized to 10 monoaromatic compounds, with the most appreciable quantities accumulated as cinnamic, benzoic, caffeic, vanillic, and ferulic acids. 2-Bromoethanesulfonic acid seemed to effectively block CH(4) formation in the anaerobic food chain, resulting in the observed buildup of volatile fatty acids and monoaromatic intermediates. Neither fatty acids nor aromatic compounds were detected in the oligolignol substrate before its metabolism, suggesting that these anaerobic consortia have the ability to mediate the cleavage of the beta-aryl-ether bond, the most common intermonomeric linkage in lignin, with the subsequent release of the observed constituent aromatic monomers.

Journal Article↗
PubMed1986

Comparative growth of natural bacterial isolates on various lignin-related compounds.

Bacterial strains were isolated on the basis of their ability to proliferate in a minimal medium containing one of a series of lignin-related compounds as the sole carbon and energy source. These included the aromatic monomers guaiacol, vanillic and coumaric acids, a dimer and a trimer possessing the arylglycerol-beta-aryl ether linkage, anisoin, and both the ether-soluble and -insoluble fractions of kraft lignin. The growth of the strains on each of these compounds was measured. The results showed that the metabolic properties of the strains varied according to the structure of the carbon sources used for their selection. Spectrophotometric tracings of the culture medium during the log phase of growth of one of the strains on the beta-O-4 dimer revealed decomposition with the release of guaiacol.

Journal Article↗
PubMed1987

Mating System and Basidiospore Formation in the Lignin-Degrading Basidiomycete Phanerochaete chrysosporium.

Prototrophic strains recovered from crosses between auxotrophic strains of the lignin-degrading basidiomycete Phanerochaete chrysosporium were induced to fruit. The progeny of most of these self-crosses were prototrophic, indicating that the nuclei of the original prototroph were wild-type recombinants rather than complementary heterokaryons and that the binucleate basidiospores of this organism are homokaryotic. Various wild-type strains were shown to have multinucleate cells lacking clamp connections and to possess a variable number of sterigmata per basidium. Colonies arising from single conidia of various wild-type strains were all capable of producing fruit bodies and basidiospores. In addition, single basidiospores from three wild-type strains all produced fruit bodies and basidiospores. Nonfruiting as well as fruiting isolates were obtained from single basidiospores of five other wild-type strains. Basidiospores from these fruiting isolates always yielded colonies that fruited, again indicating that the spores are homokaryotic. Nonfruiting isolates from the same strain did not produce basidiospores when allowed to form a heterokaryon, implying that these isolates do not represent mating types. All this evidence indicates that P. chrysosporium has a primary homothallic mating system. In addition to fruiting and nonfruiting phenotypes, basidiospores from strain OGC101, a derivative of ME-446, gave rise to colonies which did not grow on cellulose (Cel). The fruiting, nonfruiting, and Cel phenotypes differed from each other and from the parental wild-type strain in a variety of characteristics, including growth, conidiation, and evolution of CO(2) from C-side chain-labeled lignin, indicating that strain OCG101 is a heterokaryon.

Journal Article↗
PubMed1988

Control of Lignin Peroxidase Production by Phanerochaete chrysosporium INA-12 by Temperature Shifting.

There are two temperature optima connected with lignin peroxidase synthesis by Phanerochaete chrysosporium INA-12. One, at 37 degrees C, is for the mycelium-growing phase; the other, at 30 degrees C, is for the lignin peroxidase-producing phase. One of six extracellular proteins with ligninase activity increased when cultures were grown at 30 degrees C for the entire fermentation period or when cultures were grown at 37 degrees C for the first 2 days of incubation and then shifted to 30 degrees C, compared with the activity of control cultures grown at 37 degrees C for the entire fermentation period. The unsaturation of fatty acid (Delta/mole) of P. chrysosporium INA-12 mycelium decreased from 1.25 to 1.03 when the growth temperature was shifted from 20 to 40 degrees C.

Journal Article↗