Reaction kinetics of versatile peroxidase for the degradation of lignin compounds

American Journal of Biochemistry and Biotechnology

Volumn 9, Issue 4, 2013, Pages 365-394

  Busse, N ^a   Wagner, D ^a   Kraume, M ^b   Czermak, P ^a,c,d  

^a TECHNISCHE HOCHSCHULE MITTELHESSEN   (Germany)

^b TECHNISCHE UNIVERSITÄT BERLIN   (Germany)

^c Sunflower Networking Group   (United States)

^d JUSTUS LIEBIG UNIVERSITY   (Germany)

Author keywords

Deactivation; Lignin model compound (LMC); Slow transient states; Steady state kinetics; Versatile peroxidase (VP)

Indexed keywords

DEACTIVATION; LIGNIN MODEL COMPOUND; STEADY-STATE KINETICS; TRANSIENT STATE; VERSATILE PEROXIDASE;

ENZYMES; LIGNIN; REACTION KINETICS;

KINETICS;

ADLEROL; HYDROGEN PEROXIDE; LIGNIN; PEROXIDASE; UNCLASSIFIED DRUG;

ABSORPTION; ARTICLE; CHEMICAL REACTION KINETICS; CONTROLLED STUDY; DRUG DEGRADATION; ENZYME ACTIVITY; ENZYME INACTIVATION; ENZYME STABILITY; ENZYME SUBSTRATE COMPLEX; MICHAELIS MENTEN KINETICS; PH; STEADY STATE; ULTRAVIOLET SPECTROPHOTOMETRY;

EID: 84891460082     PISSN: 15533468     EISSN: None     Source Type: Journal    
DOI: 10.3844/ajbbsp.2013.365.394     Document Type: Article

References (90)

1. Acosta, M., J.A. del Río, M.B. Arnao, J. Sánchez-Bravo and F. Sabater, et al., 1988. Oxygen consumption and enzyme inactivation in the indolyl-3-acetic acid oxidation catalyzed by peroxidase. Biochimica et Biophysica Acta (BBA)-Protein Structure Mol. Enzymol., 955: 194-202. DOI: 10.1016/0167-4838(88)90193-8
2. Adler, E., 1977. Lignin chemistry-past, present and future. Wood Sci. Technol., 11: 169-218. DOI: 10.1007/BF00365615
3. Aitken, M.D. and R.L. Irvine, 1989. Stability testing of ligninase and Mn-peroxidase from Phanerochaete chrysosporium. Biotechnol. Bioeng., 34: 1251-1260. DOI: 10.1002/bit.260341003
4. Andrawis, A., K.A. Johnson and M. Tien, 1988. Studies on compound I formation of the lignin peroxidase from Phanerochaete chrysosporium. J. Biol. Chem., 263: 1195-1198. PMID: 3335539
5. Arnao, M.B., M. Acosta, J.A. del Río and F. García-Cánovas, 1990a. Inactivation of peroxidase by hydrogen peroxide and its protection by a reductant agent. Biochim. Biophys. Acta (BBA)-Protein Struct. Mol. Enzymol., 1038: 85-89. DOI: 10.1016/0167-4838(90)90014-7
6. Arnao, M.B., M. Acosta, J.A. del Río, R. Varón and F. García-Cánovas, 1990b. A kinetic study on the suicide inactivation of peroxidase by hydrogen peroxide. Biochim. Biophys. Acta (BBA)-Protein Struct. Mol. Enzymol., 1041: 43-47. DOI: 10.1016/0167- 4838(90)90120-5
7. Bakovic, M. and H.B. Dunford, 1993. Kinetics of the oxidation of p-coumaric acid by prostaglandin H synthase and hydrogen peroxide. Biochemistry, 32: 833-840. DOI: 10.1021/bi00054a014
8. Barr, D.P. and S.D. Aust, 1994. Conversion of lignin peroxidase compound III to active enzyme by cation radicals. Arch. Biochem. Biophys., 312: 511-515. DOI:10.1006/abbi.1994.1339
9. Bielski, B.H., D.E. Cabelli, L.A. Ravindra and A.B. Ross, 1985. Reactivity of HO2/O2- Radicals in aqueous solution. J. Phys. Chem. Ref. Data, 14: 1041-1100.
10. Bisswanger, H., 2008. Enzyme Kinetics: Section 2. In: Enzyme Kinetics, (Eds.), Wiley-VCH Verlag GmbH and Co. KGaA, ISBN-10: 9783527319572, pp: 124-193.
11. Böckle, B., M.J. Martínez, F. Guillén and Á.T. Martínez, 1999. Mechanism of peroxidase inactivation in liquid cultures of the ligninolytic fungus pleurotus pulmonarius. Applied Environ. Microbiol., 65: 923-928. PMCID: PMC91124
12. Cai, D. and M. Tien, 1992. Kinetic studies on the formation and decomposition of compounds II and III. Reactions of lignin peroxidase with H2O2. J. Biol. Chem., 267: 11149-11155. PMID: 1317857
13. Camarero, S., S. Sarkar, F.J. Ruiz-Dueñas, M.J. Martínez and Á.T. Martínez, 1999. Description of a versatile peroxidase involved in the natural degradation of lignin that has both manganese peroxidase and lignin peroxidase substrate interaction sites. J. Biol. Chem., 274: 10324-10330. DOI: 10.1074/jbc.274.15.10324
14. Chance, B. and A.C. Maehly, 1955. [136] Assay of Catalases and Peroxidases. 1st Edn., Methods in Enzymology, Academic Press, pp: 764-775.
15. Child, R.E. and W.G. Bradsley, 1975. The steady-state kinetics of peroxidase with 2,2'-azino-di-(3-ethyl-benzthiazoline-6-sulphonic acid) as chromogen. Biochem. J., 145: 93-103. PMCID: PMC1165190
16. Cho, D.W., R. Parthasarathi, A.S. Pimentel, G.D. Maestas and H.J. Park, et al., 2010. Nature and kinetic analysis of carbon-carbon bond fragmentation reactions of cation radicals derived from SETOxidation of lignin model compounds. J. Organic Chem., 75: 6549-6562.
17. Chung, N. and S.D. Aust, 1995. Inactivation of lignin peroxidase by hydrogen peroxide during the oxidation of phenols. Arch. Biochem. Biophys., 316: 851-855. DOI: 10.1006/abbi.1995.1114
18. Cleland, W.W., 1963. The kinetics of enzyme-catalyzed reactions with two or more substrates or products: I. Nomenclature and rate equations. Biochim. Biophys. Acta (BBA)-Specialized Section Enzymological Subjects, 67: 104-137. DOI: 10.1016/0926-6569(63)90211-6
19. Copeland, D.C., 2000. The Origins of Major War. 1st Edn., Cornell University Press, Ithaca, ISBN-10: 0801437504, pp: 322.
20. Cornish-Bowden, A., 2012. Fundamentals of Enzyme Kinetics. 1st Edn., Wiley-Blackwell, ISBN-10: 9783527330744, pp: 510.
21. Dashtban, M., H. Schraft, T.A. Syed and W. Qin, 2010. Fungal biodegradation and enzymatic modification of lignin. Int. J. Biochem. Mol. Biol., 1: 36-50. PMC: 3180040
22. Dunford, H.B., 1991. Horsradish Peroxidase: Structure and Kinetic Properties. In: Peroxidases in Chemistry and Biology, Everse, J. (Ed.), CRC Press Inc., pp: 1-24.
23. Dunford, H.B., 2010. Peroxidases and Catalases: Biochemistry, Biophysics, Biotechnology and Physiology. 1st Edn., John Wiley and Sons. ISBN-10: 9780470224762, pp: 459.
24. Eisenthal, R. and M.J. Danson, 2002. Enzyme Assays: A practical approach, Oxford University Press, USA., ISBN-10: 0199638209, pp: 302.
25. Ek, M., G. Gellerstedt and G. Henriksson, 2009. Wood Chemistry and Wood Biotechnology (Pulp and Paper Chemistry and Technology), ISBN-10: 978-3-11-021340-9, pp: 308.
26. Eriksson, K.E.L., R.A. Blanchette and P. Ander, 1990. Microbial and enzymatic degradation of wood and wood components, Springer-Verlag. pp: ix + 407
27. Garcia-Ruiz, E., D. Gonzalez-Perez, F.J. Ruiz-Dueñas, Á.T. Martínez and M. Alcalde, 2012. Directed evolution of a temperature-, peroxide- and alkaline pH-tolerant versatile peroxidase. Biochem. J., 441: 487-498. DOI: 10.1042/bj20111199
28. German, D.P., M.N. Weintraub, A.S. Grandy, C.L. Lauber and Z.L. Rinkes, et al., 2011. Optimization of hydrolytic and oxidative enzyme methods for ecosystem studies. Soil Biol. Biochem., 43: 1387-1397. DOI: 10.1016/j.soilbio.2011.03.017
29. Giardina, P., G. Palmieri, B. Fontanella, V. Rivieccio and G. Sannia, 2000. Manganese Peroxidase Isoenzymes Produced by Pleurotus ostreatus Grown on Wood Sawdust. Archives of Biochemistry and Biophysics 376: 171-179. DOI: 10.1006/abbi.1999.169
30. Goodwin, D.C., D.P. Barr, S.D. Aust and T.A. Grover, 1994. The role of oxalate in lignin peroxidase-catalyzed reduction: Protection from compound iii accumulation. Arch. Biochem. Biophys., 315: 267-272. DOI: 10.1006/abbi.1994.1499
31. Halliwell, B. and J.M.C. Gutteridge, 1985. The importance of free radicals and catalytic metal ions in human diseases. Mol. Aspects Med., 8: 89-193. DOI: 10.1016/0098- 2997(85)90001-9
32. Hammel, K.E., K.A. Jensen, M.D. Mozuch, L.L. Landucci and M. Tien, et al., 1993. Ligninolysis by a purified lignin peroxidase. J. Biol. Chem., 268: 12274-12281. PMID: 8509364
33. Harman, L.S., D.K. Carver, J. Schreiber and R.P. Mason, 1986. One- and two-electron oxidation of reduced glutathione by peroxidases. J. Biol. Chem., 261: 1642-1648. PMID: 3020935
34. Harvey, P.J., L.P. Candelas, D. Renzoni, P. Jones, P. Wardman and J.M. Palmer, 1993. Plant peroxidases: Biochemistry and physiology. Proceedings of the International Symposium of Plant Peroxidases III, Jul. 10-14, Elsinore, Denmark, University of Copenhagen and University of Geneva, pp: 185-191.
35. Hatakka, A., T. Lundell, A.L.M. Tervila-Wilo and G. Brunow, 1991. Metabolism of non-phenolic β- O-4 lignin model compounds by the white-rot fungus Phlebia radiata. Applied Microbiol. Biotechnol., 36: 270-277. DOI: 10.1007/BF00164433
36. Howard, R.L., E. Abotsi, E.L. Jansen van Rensburg and S. Howard, 2003. Lignocellulose biotechnology: Issues of bioconversion and enzyme production. African J. Biotechnol., 2: 602-619.
37. Hu, Z.C., R.A. Korus, C.R. Venkataramu and R.L. Crawford, 1993. Deactivation kinetics of lignin peroxidase from Phanerochaete chrysosporium. Enzyme Microbial. Technol., 15: 567-574. DOI: 10.1016/0141-0229(93)90018-W
38. Jantschko, W., P.G. Furtmuller, M. Zederbauer, K. Neugschwandtner and C. Jakopitsch, et al., 2005. Reaction of ferrous lactoperoxidase with hydrogen peroxide and dioxygen: An anaerobic stopped-flow study. Arch. Biochem. Biophys., 434: 51-59.
39. Jena Bioscience, 2010. Data Sheet Versatile Peroxidase EC 1.11.1.16, Mn(II): H2O2 oxidoreductase/diarylpropane: O2, H2O2 oxidoreductase, Bjerkandera adusta.
40. Kamm, B., M. Kamm, P.R. Gruber and S. Kromus, 2008. Biorefinery Systems-An Overview. 1st Edn., Biorefineries-Industrial Processes and Products, (Eds.), Wiley-VCH Verlag GmbH, pp: 1-40.
41. Kanofsky, J.R., 1991. Peroxidase-Catalyzed Generation of Singlet Oxygen and of Free Radicals. In: Peroxidases in chemistry and biology. Everse, J., (Eds.), CRC Press Inc., pp: 219-237.
42. Kettle, A.J., R.F. Anderson, M.B. Hampton and C.C. Winterbourn, 2007. Reactions of Superoxide with Myeloperoxidase Biochem., 46: 4888-4897. DOI: 10.1021/bi602587k
43. Kirk, T.K. and R.L. Farrell, 1987. Enzymatic combustion: The microbial degradation of lignin. Annu. Rev. Microbiol., 41: 465-505. DOI: 10.1146/annurev.mi.41.100187.002341
44. Kirk, T.K., M. Tien, P.J. Kersten, M.D. Mozuch and B. Kalyanaraman, 1986. Ligninase of Phanerochaete chrysosporium. Mechanism of its degradationof the non-phenolic arylglycerol betaaryl ether substructure of lignin. Biochem. J., 236: 279-287. PMCID: PMC1146817
45. Kulmacz, R.J., 1986. Prostaglandin H synthase and hydroperoxides: Peroxidase reaction and inactivation kinetics. Arch. Biochem. Biophys., 249: 273-285. DOI: 10.1016/0003- 9861(86)90003-2
46. Lange, J.P., 2007. Lignocellulose conversion: An introduction to chemistry, process and economics. Biofuels, Bioproducts Biorefin., 1: 39-48. DOI: 10.1002/9783527621118.ch2
47. Liers, C., C. Bobeth, M. Pecyna, R. Ullrich and M. Hofrichter, 2010. DyP-like peroxidases of the jelly fungus Auricularia auricula-judae oxidize nonphenolic lignin model compounds and highredox potential dyes. Applied Microbiol. Biotechnol., 85: 1869-1879. DOI: 10.1007/s00253-009-2173-7
48. Lundell, T., H. Schoemaker, A. Hatakka and G. Brunow, 1993a. New mechanism of the Cα-Cβ cleavage in non-phenolic arylglycerol β-aryl ether lignin substructures catalyzed by lignin peroxidase. Holzforschung-Int. J. Biol. Chem. Phys. Technol. Wood, 47: 219. DOI: 10.1515/hfsg.1993.47.3.219
49. Lundell, T., R. Wever, R. Floris, P. Harvey and A. Hatakka, et al., 1993b. Lignin peroxidase L3 from Phlebia radiata. Pre-steadystate and steady-state studies with veratryl alcohol and a non-phenolic lignin model compound 1-(3,4-dimethoxyphenyl)-2-(2- methoxyphenoxy)propane-1,3-diol. Eur. J. Biochem., 211: 391-402.
50. Marangoni, A.G., 2003. Enzyme Kinetics: A Modern Approach. 1st Edn., Wiley-Interscience. ISBN-10: 0471461415, pp: 229.
51. Martínez, A.T., 2007. High Redox Potential Peroxidases. 1st Edn., Industrial Enzymes. Polaina, J. and A. Mac- Cabe, (Eds.), Springer Netherlands, ISBN-10: 9781402053771, pp: 477-488.
52. Martínez, A.T., M. Speranza, F.J. Ruiz-Dueñas, P. Ferreira and S. Camarero, et al., 2005. Biodegradation of lignocellulosics: Microbial, chemical and enzymatic aspects of the fungal attack of lignin. Int. Microbiol., 8: 195-204. PMID: 16200498
53. Martínez, M.J., F.J. Ruiz-Dueñas, F. Guillén and Á.T. Martínez, 1996. Purification and catalytic properties of two manganese peroxidase isoenzymes from Pleurotus eryngii. Europ. J. Biochem., 237: 424-432. DOI:10.1111/j.1432-1033.1996.0424k.x
54. Mester, T. and J.A. Field, 1998. Characterization of a Novel Manganese Peroxidase-Lignin Peroxidase Hybrid Isozyme Produced by Bjerkandera Species Strain BOS55 in the Absence of Manganese. J. Biol. Chem., 273: 15412-15417. DOI: 10.1074/jbc.273.25.15412
55. Moreira, P.R., F. Bouillenne, E. Almeida-Vara, F. Xavier Malcata, J.M. Frere and J.C. Duarte, 2006. Purification, kinetics and spectral characterisation of a new versatile peroxidase from a Bjerkandera sp. isolate. Enzyme Icrobial Echnol., 38: 28-33. DOI: 10.1016/j.enzmictec.2004.12.035
56. Nakajima, R. and I. Yamazaki, 1987. The mechanism of oxyperoxidase formation from ferryl peroxidase and hydrogen eroxide. J. Biol. Chem., 262: 2576-2581. PMID: 3029087
57. Nakamura, M., I. Yamazaki, T. Kotani and S. Ohtaki, 1985. Thyroid peroxidase selects the mechanism of either 1- or 2- lectron oxidation of phenols, depending on their substituents. J. Biol. Chem., 260: 13546-13552. PMID: 2997169
58. Nicell, J.A., J.K. Bewtra, N. Biswas and E. Taylor, 1993. Reactor development for peroxidase catalyzed polymerization nd precipitation of phenols from wastewater. Water Res., 27: 1629-1639. DOI: 10.1016/0043-1354(93)90127-4
59. Palmer, J.M., P.J. Harvey and H.E. Schoemaker, 1987. The role of Peroxidases, Radical Cations and Oxygen in the egradation of Lignin [and Discussion]. Phil. Trans. R. Soc. Lond. A 321: 495-505. DOI: 10.1098/rsta.1987.0027
60. Pérez-Boada, M., F.J. Ruiz-Duenas, R. Pogni, R. Basosi and T. Choinowski, et al., 2005. Versatile peroxidase oxidation of high redox potential aromatic compounds: Site-directed mutagenesis, pectroscopic and crystallographic investigation of three long-range electron transfer pathways. J. Mol. Biol., 354: 385-402. DOI: 10.1016/j.jmb.2005.09.047
61. Pogni, R, M.C. Baratto, S. Giansanti, C. Teutloff and J. Verdin et al, 2005. Tryptophan-based radical in the catalytic mechanism of versatile peroxidase from jerkandera adusta. Biochemistry, 44: 4267-4274. DOI: 10.1021/bi047474l
62. Promega, 2009. Calculating Nucleic Acid or Protein Concentration Using the GloMax® Multi+ Microplate Instrument. Last modified date July 07, 2009
63. Rasmussen, C.B., H.B. Dunford and K.G. Welinder, 1995. Rate enhancement of compound i formation of barley eroxidase by ferulic acid, caffeic acid and coniferyl alcohol. Biochemistry, 34: 4022-4029. DOI: 10.1021/bi00012a021
64. Ruiz-Dueñas, F.J., M. Morales, E. Garcia, Y. Miki and M.J. Martínez et al, 2009a. Substrate oxidation sites in versatile peroxidase and other basidiomycete peroxidases. J. Exp. Bot, 60: 441-452. DOI: 10.1093/jxb/ern261
65. Ruiz-Dueñas, F.J., M.J. Martínez and Á.T. Martínez, 1999. Molecular characterization of a novel peroxidase isolated from the ligninolytic fungus Pleurotus eryngii. Mol. Microbiol, 31: 223-235. DOI:10.1046/j. 1365- 2958.1999.01164.x
66. Ruiz-Dueñas, F.J., R. Pogni, M. Morales, S. Giansanti and M.J. Mate et al, 2009b. Protein radicals in fungal versatile peroxidase: Catalytic tryptophan radical in both compound i and compound ii and studies on W164Y, W164H and W164S Variants. J. Biol. Chem, 284: 7986-7994. DOI: 10.1074/jbc.M808069200
67. SAC, 2012. Enabling science to improve the quality of life. Sigma-Aldrich Co. LLC.
68. Sánchez, C, 2009. Lignocellulosic residues: Biodegradation and bioconversion by fungi. Biotechnol. Adv., 27: 185-194. DOI: 10.1016/j.biotechadv.2008.11.001
69. Schoemaker, HE. and K. Piontek, 1996. On the interaction of lignin peroxidase with lignin. Pure Applied Chem., 8: 2089-2096. DOI: 10.1351/pac199668112089
70. Schoemaker, H.E., 1990. On the chemistry of lignin biodegradation. Recueil des Travaux Chimiques des Pays-Bas, 109: 255-272. DOI: 10.1002/recl. 19901090402
71. Schoemaker, HE., T.K. Lundell, A.I. Hatakka and K. Piontek, 1994b. The oxidation of veratryl alcohol, dimeric lignin models and lignin by lignin peroxidase: The redox cycle revisited. FEMS Microbiol. Rev., 13: 321-331. DOI: 10.1111/j. 1574-6976.1994.tb00052.x
72. Schoemaker, H.E., T.K. Lundell, R. Floris, T. Glumoff and K.H. Winterhalter, et al., 1994a. Do carbohydrates play a role in the lignin peroxidase cycle? Redox catalysis in the endergonic region of the driving force. Bioorganic Med. Chem., 2: 509-519. DOI: 10.1016/0968-0896(94)80021-9
73. Sinsabaugh, R.L., 2010. Phenol oxidase, peroxidase and organic matter dynamics of soil. Soil Biol. Biochem., 42: 391-404. DOI: 10.1016/j.soilbio.2009.10.014
74. Smith, A.M., W.L. Morrison and P.J. Milham, 1982. Oxidation of indole-3-acetic acid by peroxidase: Involvement of reduced peroxidase and compound III with superoxide as a product. Biochemistry, 21: 4414-4419. DOI: 10.1021/bi00261a034
75. Smith, A.T., S.A. Sanders, R.N. Thorneley, J.F. Burke and R.R. Bray, 1992. Characterisation of a haem active-site mutant of horseradish peroxidase, Phe41- ---Val, with altered reactivity towards hydrogen peroxide and reducing substrates. Eur. J. Biochem., 207: 507-519. DOI: 10.1111/j.1432-1033.1992.tb17077.x
76. Snook, M.E. and G.A. Hamilton, 1974. Oxidation and fragmentation of some phenyl-substituted alcohols and ethers by peroxydisulfate and Fenton's reagent. J. Am. Chem. Soc., 96: 860-869. DOI: 10.1021/ja00810a035
77. Stöcker, M., 2008. Bio- und BTL-Kraftstoffe in der Bioraffinerie: Katalytische Umwandlung Lignocellulose- reicher Biomasse mit porosen Stoffen. Angewandte Chem., 120: 9340-9351. DOI: 10.1002/ange.200801476
78. Tamura, M. and I. Yamazaki, 1972. Reactions of the oxyform of horseradish peroxidase. J. Biochem., 71: 311-319. PMID: 5016264
79. Tien, M. and T.K. Kirk, 1984. Lignin-degrading enzyme from Phanerochaete chrysosporium: Purification, characterization and catalytic properties of a unique H2O2-requiring oxygenase. PNAS, 81: 2280-2284. DOI:10.1073/pnas.81.8.2280
80. Tien, M., 1987. Properties of Ligninase from Phanerochaete Chrysosporium and their possible applications. Critical Rev. Microbiol., 15: 141-168. DOI: 10.3109/10408418709104456
81. Torres, E. and M. Ayala, 2010. Biocatalysis Based on Heme Peroxidases. 1st Edn., Springer, ISBN-10: 3642126278, pp: 325.
82. Valderrama, B. and R. Vazquez-Duhalt, 2005. Electronbalance during the oxidative self- inactivation of cytochrome c. J. Mol. Catalysis B: Enzymatic, 35: 41-44. DOI: 10.1016/j.molcatb.2005.05.003
83. Valderrama, B., M. Ayala and R. Vazquez-Duhalt, 2002. Suicide inactivation of peroxidases and the challenge of engineering more robust enzymes. Chem. Biol., 9: 555-565. DOI: 10.1016/S1074-5521(02)00149-7
84. van Rantwijk, F. and R.A. Sheldon, 2000. Selective oxygen transfer catalysed by heme peroxidases: Synthetic and mechanistic aspects. Curr. Opinion Biotechnol., 11: 554-564. DOI: 10.1016/S0958-1669(00)00143-9
85. Villas-Bôas, S.G., E. Esposito and D.A. Mitchell, 2002. Microbial conversion of lignocellulosic residues for production of animal feeds. Ani. Feed Sci. Technol., 98: 1-12. DOI: 10.1016/S0377-8401(02)00017-2
86. Vlasits, J., C. Jakopitsch, M. Bernroitner, M. Zamocky, P.G. Furtmuller and C. Obinger, 2010. Mechanisms of catalase ctivity of heme peroxidases. Arch. Biochem. Biophys., 500: 74-81. DOI: 10.1016/j.abb.2010.04.018
87. Wang, Y., R. Vazquez-Duhalt and M.A. Pickard, 2003. Manganese-lignin peroxidase hybrid from Bjerkandera adusta oxidizes polycyclic aromatic hydrocarbons more actively in the absence of manganese. Canadian J. Microbiol., 49: 675-682. DOI: 10.1139/w03-091
88. Wariishi, H. and M.H. Gold, 1990. Lignin peroxidase compound III. Mechanism of formation and decomposition. J. Biol. Chem., 265: 2070-2077. PMID: 2298739
89. Wong, D.W., 2009. Structure and action mecha nism of ligninolytic enzymes. Applied Biochem. Biotechnol., 157: 174-209. DOI: 10.1007/s12010-008- 8279-z
90. Yokota, K. and I. Yamazaki, 1965. The activity of the horseradish peroxidase compound 3. Biochem. Biophys. Res. Commun., 18: 48-53. DOI: 10.1016/0006-291X(65)90880-6