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2007 | 5 | 3 | 672-687

Article title

Mechanistic studies on the effect of veratryl alcohol on the lignin peroxidase catalyzed oxidation of pyrogallol red in reversed micelles


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The lignin peroxidase (LiP) catalyzed oxidation of pyrogallol red (PR) in the absence and presence of veratryl alcohol (3,4-dimethoxybenzyl alcohol, VA) was carried out in bis (2-ethylhexyl) sulfosuccinate sodium (AOT)/ polyoxyethylene lauryl ether (Brij30) reversed micelles to elucidate the role of VA. Results indicated that VA could accelerate the LiP catalyzed oxidation of PR, especially at low H2O2 concentrations. Unlike in bulk aqueous medium, the protection of LiP by VA in the present medium was relatively unsubstantial, even at high H2O2 concentrations. Analysis of data from a series of experiments showed that the enhancement of the PR oxidation caused by VA was mainly due to the indirect oxidation of PR by VA+∙ from the LiP catalyzed oxidation of VA. It was also found that at the same protector concentration (40 μM), VA (the physiological substrate of LiP) was less effective than PR (a phenolic compound) in protecting LiP from the H2O2 derived inactivation. This novel phenomenon deserves further study. [...]










Physical description


1 - 9 - 2007
9 - 6 - 2007


  • Key Laboratory of Colloid Interface Chemistry of the Education Ministry of China, Shandong University, Jinan, 250100, P.R. China
  • State Key Laboratory of Microbial Technology of China, Shandong University, Jinan, 250100, P.R. China
  • State Key Laboratory of Microbial Technology of China, Shandong University, Jinan, 250100, P.R. China
  • State Key Laboratory of Microbial Technology of China, Shandong University, Jinan, 250100, P.R. China
  • State Key Laboratory of Microbial Technology of China, Shandong University, Jinan, 250100, P.R. China
  • State Key Laboratory of Microbial Technology of China, Shandong University, Jinan, 250100, P.R. China


  • [1] J.A. Bumpus, M. Tien, D. Wright and S.D. Aust: “Oxidation of persistent environmental pollutants by a white rot fungus”, Science, Vol. 228, (1985), pp. 1434–1436. http://dx.doi.org/10.1126/science.3925550[Crossref]
  • [2] D.P. Barr and S.D. Aust: “Mechanisms white rot fungi use to degrade pollutants”, Environ. Sci. Technol., Vol. 28, (1994), pp. 78A–87A. http://dx.doi.org/10.1021/es00051a002[Crossref]
  • [3] B.W. Bogan and R.T. Lamar: “One-electron oxidation in the degradation of creosote polycyclic aromatic hydrocarbons by Phanerochaete chrysosporium”, Appl. Environ. Microbiol., Vol. 61, (1995), pp. 2631–2635.
  • [4] S. Sayadi and R. Ellouz: “Roles of lignin peroxidase and manganese peroxidase from Phanerochaete chrysosporium in the decolorization of olive mill wastewaters”, Appl. Environ. Microbiol., Vol. 61, (1995), pp. 1098–1103.
  • [5] Z. Zheng and J.P. Obbard: “Oxidation of polycyclic aromatic hydrocarbons (PAH) by the white rot fungus Phanerochaete chrysosporium”, Enzym. Microb. Technol., Vol. 31, (2002), pp. 3–9. http://dx.doi.org/10.1016/S0141-0229(02)00091-1[Crossref]
  • [6] D. Wesenberg, I. Kyriakides and S.N. Agathos: “White-rot fungi and their enzymes for the treatment of industrial dye effluents”, Biotechnol. Adv., Vol. 22, (2003), pp. 161–187. http://dx.doi.org/10.1016/j.biotechadv.2003.08.011[Crossref]
  • [7] H. Hirai, S. Nakanishi and T. Nishida: “Oxidative dechlorination of methoxychlor by ligninolytic enzymes from white-rot fungi”, Chemosphere, Vol. 55, (2004), pp. 641–645. http://dx.doi.org/10.1016/j.chemosphere.2003.11.035[Crossref]
  • [8] K.E. Hammel, B. Kalyanaraman and T.K. Kirk: “Oxidation of polycyclic aromatic hydrocarbons and dibenzo[p]-dioxins by Phanerochaete chrysosporium ligninase”, J. Biol. Chem., Vol. 261, (1986), pp. 16948–16952.
  • [9] R.S. Koduri and M. Tien: “Oxidation of guaiacol by lignin peroxidase”, J. Biol. Chem., Vol. 270, (1995), pp. 22254–22258. http://dx.doi.org/10.1074/jbc.270.38.22254[Crossref]
  • [10] M. Tien and D. Ma: “Oxidation of 4-methoxymandelic acid by lignin peroxidase. Mediation by veratryl alcohol”, J. Biol. Chem., Vol. 272, (1997), pp. 8912–8917. http://dx.doi.org/10.1074/jbc.272.14.8912[Crossref]
  • [11] T. Mester, K. Ambert-Balay, S. Ciofi-Baffoni, L. Banci, A.D. Jones and M. Tien: “Oxidation of a tetrameric nonphenolic lignin model compound by lignin peroxidase”, J. Biol. Chem., Vol. 276, (2001), pp. 22985–22990. http://dx.doi.org/10.1074/jbc.M010739200[Crossref]
  • [12] E. Baciocchi, C. Fabbri and O. Lanzalunga: “Lignin peroxidase-catalyzed oxidation of nonphenolic trimeric lignin model compounds: fragmentation reactions in the intermediate radical cations”, J. Org. Chem., Vol. 68, (2003), pp. 9061–9069. http://dx.doi.org/10.1021/jo035052w[Crossref]
  • [13] G. Ward, Y. Hadar, I. Bilkis and C.G. Dosoretz: “Mechanistic features of lignin peroxidase-catalyzed oxidation of substituted phenols and 1,2-dimethoxyarenes”, J. Biol. Chem., Vol. 278, (2003), pp. 39726–39734. http://dx.doi.org/10.1074/jbc.M303918200[Crossref]
  • [14] X. Huang, D. Wang, C. Liu, M. Hu, Y. Qu and P. Gao: “The roles of veratryl alcohol and nonionic surfactant in the oxidation of phenolic compounds by lignin peroxidase”, Biochem. Biophys. Res. Commun., Vol. 311, (2003), pp. 491–494. http://dx.doi.org/10.1016/j.bbrc.2003.10.029[Crossref]
  • [15] J. Lan, X. Huang, M. Hu, Y. Li, Y. Qu, P. Gao and D. Wu: “High efficient degradation of dyes with lignin peroxidase coupled with glucose oxidase”, J. Biotechnol., Vol. 123, (2006), pp. 483–490. http://dx.doi.org/10.1016/j.jbiotec.2005.12.034[Crossref]
  • [16] M. Oyadomari, H. Shinohara, T. Johjima, H. Wariishi and H. Tanaka: “Electrochemical characterization of lignin peroxidase from the white-rot basidiomycete Phanerochaete chrysosporium”, J. Mol. Catal. B: Enzym., Vol. 21, (2003), pp. 291–297. http://dx.doi.org/10.1016/S1381-1177(02)00256-4[Crossref]
  • [17] M. Ayala Aceves, M.C. Baratto, R. Basosi, R. Vazquez-Duhalt and R. Pogni: “Spectroscopic characterization of a manganese-lignin peroxidase hybrid isozyme produced by Bjerkandera adusta in the absence of manganese: evidence of a protein centred radical by hydrogen peroxide”, J. Mol. Catal. B: Enzym., Vol. 16, (2001), pp. 159–167. http://dx.doi.org/10.1016/S1381-1177(01)00056-X[Crossref]
  • [18] K. Martinek, A.V. Levashov, N.L. Klyachko, Y.L. Khmelnitski and I.V. Berezin: “Micellar enzymology”, Eur. J. Biochem., Vol. 155, (1986), pp. 453–468. http://dx.doi.org/10.1111/j.1432-1033.1986.tb09512.x[Crossref]
  • [19] P.L. Luisi: “Enzyme hosted in reversed micelles in hydrocarbon solution”, Angrew. Chem., Vol. 24, (1985), pp. 439–450. http://dx.doi.org/10.1002/anie.198504393[Crossref]
  • [20] W. Zhang, X. Huang, Y. Li, Y. Qu and P. Gao: “Catalytic activity of lignin peroxidase and partitioning of veratryl alcohol in AOT/isooctane/water reverse micelles”, Appl. Microbiol. Biotechnol., Vol. 70, (2006), pp. 315–320. http://dx.doi.org/10.1007/s00253-005-0048-0[Crossref]
  • [21] M. Kimura, J. Michizoe, S. Oakazaki, S. Furusaki, M. Goto, H. Tanaka and H. Wariishi: “Activation of lignin peroxidase in organic media by reversed micelles”, Biotechnol. Bioeng., Vol. 88, (2004), pp. 495–501. http://dx.doi.org/10.1002/bit.20277[Crossref]
  • [22] D. Chen and M. Liao: “Effects of mixed reverse micellar structure on stability and activity of yeast alcohol dehydrogenase”, J. Mol. Catal. B: Enzym., Vol. 18, (2002), pp. 155–162. http://dx.doi.org/10.1016/S1381-1177(02)00080-2[Crossref]
  • [23] T. Johjima, H. Wariishi and H. Tanaka: “Veratryl alcohol binding sites of lignin peroxidase from Phanerochaete chrysosporium”, J. Mol. Catal. B: Enzym., Vol. 17, (2002), pp. 49–57. [Crossref]
  • [24] P.J. Harvey, H.E. Schoemaker and J.M. Palmer: “Veratryl alcohol as a mediator and the role of radical cations in lignin biodegradation by Phanerochaete chrysosporium”, FEBS Lett., Vol. 195, (1986), pp. 242–246. http://dx.doi.org/10.1016/0014-5793(86)80168-5[Crossref]
  • [25] A. Khindaria, G. Nie and S.D. Aust: “Detection and characterization of the lignin peroxidase compound II-veratryl alcohol cation radical complex”, Biochemistry, Vol. 36, (1997), pp. 14181–14185. http://dx.doi.org/10.1021/bi9715730[Crossref]
  • [26] D. Sheng and M.H. Gold: “Irreversible oxidation of ferricytochrome c by lignin peroxidase”, Biochemistry, Vol. 37, (1998), pp. 2029–2036. http://dx.doi.org/10.1021/bi972198e[Crossref]
  • [27] K. Won, Y.H. Kim, E.S. An, Y.S Lee and B.K. Song: “Horseradish peroxidase-catalyzed polymerization of cardanol in the presence of redox mediators”, Biomacromolecules, Vol. 5, (2004), pp. 1–4. http://dx.doi.org/10.1021/bm034325u[Crossref]
  • [28] J. Lan, F. Wang, X. Huang, Y. Li, Y. Qu and P. Gao: “Studies on the hydrogen peroxide regulated veratryl alcohol mediated oxidation of pyrogallol red catalyzed by lignin peroxidase”, Acta Chim. Sin., Vol. 64, (2006), pp. 463–468.
  • [29] Y. Li, P. Gao and Z. Wang: “Nutritional regulation of synthesis of lignin peroxidase by Phanerochaete chrysosporium ME-446”, Acta Microbiol. Sin., Vol. 34, (1994), pp. 29–36.
  • [30] M.J. Selwyn: “A simple test for inactivation of an enzyme during assay”, Biochim. Biophys. Acta, Vol. 105, (1965), pp. 193–195.
  • [31] H. Wariishi and M.H. Gold: “Lignin peroxidase compound III. Mechanism of formation and decomposition”, J. Biol. Chem., Vol. 265, (1990), pp. 2070–2077.
  • [32] H. Wariishi and M.H. Gold: “Lignin peroxidase compound III: formation, inactivation, and conversion to the native enzyme”, FEBS Lett., Vol. 243, (1989), pp. 165–168. http://dx.doi.org/10.1016/0014-5793(89)80122-X[Crossref]
  • [33] D. Cai and M. Tien: “Kinetic studies on the formation and decomposition of compounds II and III reactions of lignin peroxidase with H2O2”, J. Biol. Chem., Vol. 267, (1992), pp. 11149–11155.
  • [34] N. Chung and S.D. Aust: “Inactivation of lignin peroxidase by hydrogen peroxide during the oxidation of phenols”, Arch. Biochem. Biophys., Vol. 316, (1995), pp. 851–855. http://dx.doi.org/10.1006/abbi.1995.1114[Crossref]

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