Lignin peroxidase compound III

Wariishi, Hiroyuki; Gold, Michael H.

doi:10.1016/0014-5793(89)80122-x

Cited by 103 publications

(24 citation statements)

References 18 publications

(25 reference statements)

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“…The formation of superoxide anion during veratryl alcohol oxidation was postulated by Haemmerli et al [22] to explain lactone and quinone formation. Recently Wariishi et al [31] showed the release of OzjHO; from lignin peroxidase compound 111 in the presence of veratryl alcohol.…”

Section: Resultsmentioning

confidence: 99%

Effect of Mn(II) on reactions catalyzed by lignin peroxidase from Phanerochaete chrysosporium

Bono¹,

Goulas²,

Boe³

et al. 1990

European Journal of Biochemistry

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The effect of manganese on lignin peroxidase activity was studied. The enzyme was produced with a new process using an air-lift-type reactor. The experiments were performed with veratryl alcohol and a dimeric lignin model compound. It was shown that when Mn(I1) . lactate complex was present the amount of veratraldehyde formed and the uptake of oxygen were significantly enhanced during the aerobic oxidation of veratryl alcohol. A similar effect can be obtained with superoxide dismutase. These results strongly suggest that the superoxide anion can occur during the reaction; its scavenging by Mn(I1) or superoxide dismutase generates H202. In contrast, no evidence for the formation of superoxide anion was found during oxidation of the lignin model, compound veratrylglycerol-/3-guaiacyl ether.The discovery of the extracellular ligninolytic system of the white-rot fungus Phanerochaete chrysosporium [1, 21 has renewed interest in biodelignification. The constituents of this system have been identified as two types of peroxidase, now referred to as lignin peroxidase or ligninase, and manganesedependent peroxidase. Recently, Kersten et al. [3] demonstrated an H202-generating system, a glyoxal oxidase in ligninolytic cultures.Lignin peroxidase is able to catalyse a variety of reactions in lignin model compounds. This enzyme functions by singleelectron oxidation, leading to cation radical intermediates [4, 51; their further decomposition and the evolution of the radical-moiety depend on their chemical structure [6 -91. Such a mechanism could explain the non-specificity of lignin-peroxidase-catalyzed reactions, and makes this enzyme important for lignin depolymerisation.The activity of manganese-dependent peroxidase toward phenolic substrates depends on the presence of manganese [lo, 111. This peroxidase oxidizes Mn(I1) to Mn(III), which is in fact the effective oxidative agent involved in the enzymic reactions [12].As lignin is a complex polymer, its biodegradation may require some synergy between enzymes. In this paper, we examine if manganese also has an effect on lignin peroxidase activity. For this purpose, lignin peroxidase was isolated from the culture fluid of P. chrysosporium grown in an air-lift-type reactor, with a glycerol/high-nitrogen-supplemented medium. The experiments were performed with two substrates, veratryl alcohol, a secondary metabolite produced by the fungus during lignin biodegradation [13], and veratrylglycerol-P-guaiacyl ether, a dimeric lignin model compound.

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Section: Resultsmentioning

confidence: 99%

Effect of Mn(II) on reactions catalyzed by lignin peroxidase from Phanerochaete chrysosporium

Bono¹,

Goulas²,

Boe³

et al. 1990

European Journal of Biochemistry

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“…Veratryl alcohol has been shown to protect lignin peroxidase from H 2 O 2 -dependent inactivation (11,30); it has been shown to prevent compound III accumulation (9); and it has been proposed to act as a redox mediator in lignin depolymerization (12). Strong arguments can be made for the physiological significance of the first two roles, whereas the latter role as a redox mediator has been contested.…”

Section: Reaction Of Guaiacol In Incubations Containingmentioning

confidence: 99%

“…It is also well documented that prolonged incubation of enzyme with H 2 O 2 in the absence of a reducing substrate such as veratryl alcohol can cause irreversible inactivation of the enzyme (9). In the presence of veratryl alcohol, however, lignin peroxidase undergoes multiple turnovers without any detectable inactivation.…”

mentioning

confidence: 99%

Complexes of Adenovirus with Polycationic Polymers and Cationic Lipids Increase the Efficiency of Gene Transfer in Vitro and in Vivo

Fasbender

Zabner²,

Chillón

et al. 1997

Journal of Biological Chemistry

248

218

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We have investigated the lignin peroxidase-catalyzed oxidation of guaiacol and the role of veratryl alcohol in this reaction by steady-state and pre-steady-state methods. Pre-steady-state kinetic analyses demonstrated that guaiacol is a good substrate for both compounds I and II, the two-and one-electron oxidized enzyme intermediates, respectively, of lignin peroxidase. The rate constant for the reaction with compound I is 1.2 ؋ 10 6 M ؊1 s ؊1. The reaction of guaiacol with compound II exhibits a K d of 64 M and a first-order rate constant of 17 s ؊1 . Oxidation of guaiacol leads to tetraguaiacol formation. This reaction exhibits classical Michaelis-Menten kinetics with a K m of 160 M and a k cat of 7.7 s ؊1. Veratryl alcohol, a secondary metabolite of ligninolytic fungi, is capable of mediating the oxidation of guaiacol. This was shown by steady-state inhibition studies. Guaiacol completely inhibited the oxidation of veratryl alcohol, whereas veratryl alcohol had no corresponding inhibitory effect on guaiacol oxidation. In fact, at low guaiacol concentrations, veratryl alcohol stimulated the rate of guaiacol oxidation. These results collectively demonstrate that veratryl alcohol can serve as a mediator for phenolic substrates in the lignin peroxidase reaction.This study investigates the ability of 3,4-dimethoxybenzyl (veratryl) alcohol to mediate the lignin peroxidase-catalyzed oxidation of guaiacol. Lignin peroxidases are hemeproteins secreted by the white rot fungus Phanerochaete chrysosporium during secondary metabolism (1, 2). These isozymes catalyze the oxidation of lignin and a large number of phenolic and non-phenolic substrates (3, 4). The catalytic cycle of lignin peroxidase is similar to that of other peroxidases (5, 6) where ferric enzyme is first oxidized by H 2 O 2 to generate the twoelectron oxidized intermediate, compound I (7). Compound I is then reduced by one electron donated by a substrate molecule, yielding the 1-electron oxidized enzyme intermediate, compound II, and a free radical product. The catalytic cycle is completed by the one-electron reduction of compound II by a second substrate molecule.In the absence of a reducing substrate, the enzyme can undergo a series of reactions with H 2 O 2 to form compound III, oxyperoxidase (6,8). It is also well documented that prolonged incubation of enzyme with H 2 O 2 in the absence of a reducing substrate such as veratryl alcohol can cause irreversible inactivation of the enzyme (9). In the presence of veratryl alcohol, however, lignin peroxidase undergoes multiple turnovers without any detectable inactivation. Because veratryl alcohol is normally produced by ligninolytic cultures of P. chrysosporium (10), workers have proposed that its physiological function is to protect the enzyme from H 2 O 2 -dependent inactivation (11).An alternate role for veratryl alcohol in lignin biodegradation has been proposed by Harvey et al. (12). These workers observed that substrates that are not oxidized by lignin peroxidase such as anisyl alcohol and 4-methoxyman...

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“…This happens in the absence of reductant substrates or with a high oxidant/reductant ratio (2,3,6,7,11,24,(27)(28)(29).…”

Section: Biochemistry and Molecular Biology Internationalmentioning

confidence: 99%

Role of the reductant substrates on the inactivation of horseradish peroxidase by m‐Chloroperoxybenzoic acid

1996

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SUMMARYHorseradish peroxidase reacts with H202 and other hydroperoxides to form Compound I, the first active enzymatic form. m-Chloroperoxybenzoic acid, a xenobiotic hydroperoxide, acts as an oxidant substrate of horseradish peroxidase. However, this hydroperoxide is also a powerful inactivator of the enzyme and in this sense is more effective than H202. The coupled reductant substrates used in the peroxidatic reaction protect the enzyme from the inactivating process.A reaction mechanism is proposed with two competitive routes: one catalytic and one inactivating. Using a kinetic approach, the ratio between the hydroperoxide and the reductant substrate appears to be a decisive factor in the catalytic turnover of the enzyme.The role of the reductant substrates in protecting the enzyme, and the physiological and biotechnological implications of this process are discussed.

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Lignin peroxidase compound III

Cited by 103 publications

References 18 publications

Effect of Mn(II) on reactions catalyzed by lignin peroxidase from Phanerochaete chrysosporium

Effect of Mn(II) on reactions catalyzed by lignin peroxidase from Phanerochaete chrysosporium

Complexes of Adenovirus with Polycationic Polymers and Cationic Lipids Increase the Efficiency of Gene Transfer in Vitro and in Vivo

Role of the reductant substrates on the inactivation of horseradish peroxidase by m‐Chloroperoxybenzoic acid

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