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Volumn 66, Issue 1, 2000, Pages 170-175

Oxygen activation during oxidation of methoxyhydroquinones by laccase from Pleurotus eryngii

Author keywords

[No Author keywords available]

Indexed keywords

HYDROGEN PEROXIDE; HYDROQUINONE DERIVATIVE; LACCASE; OXYGEN; SEMIQUINONE; SUPEROXIDE; SUPEROXIDE DISMUTASE;

EID: 0343415716     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.66.1.170-175.2000     Document Type: Article
Times cited : (103)

References (51)
  • 1
    • 0020118402 scopus 로고
    • The scavenging of superoxide radical by manganous complexes: In vitro
    • Archibald, F. S., and I. Fridovich. 1982. The scavenging of superoxide radical by manganous complexes: in vitro. Arch. Biochem. Biophys. 214:452-463.
    • (1982) Arch. Biochem. Biophys. , vol.214 , pp. 452-463
    • Archibald, F.S.1    Fridovich, I.2
  • 2
    • 0040018725 scopus 로고
    • Hydroxyl radical activity associated with the growth of white-rot fungi
    • Backa, S., J. Gierer, T. Reitberger, and T. Nilsson. 1993. Hydroxyl radical activity associated with the growth of white-rot fungi. Holzforschung 47:181-187.
    • (1993) Holzforschung , vol.47 , pp. 181-187
    • Backa, S.1    Gierer, J.2    Reitberger, T.3    Nilsson, T.4
  • 3
    • 37049158774 scopus 로고
    • Derivatives of pentahydroxybenzene, and a synthesis of pedicellin
    • Baker, W. 1941. Derivatives of pentahydroxybenzene, and a synthesis of pedicellin. J. Chem. Soc. 1941:662-670.
    • (1941) J. Chem. Soc. , vol.1941 , pp. 662-670
    • Baker, W.1
  • 4
    • 0026488242 scopus 로고
    • Production of hydroxyl radical by lignin peroxidase from Phanerochaete chrysosporium
    • Barr, D. P., M. M. Shah, T. A. Grover, and S. D. Aust. 1992. Production of hydroxyl radical by lignin peroxidase from Phanerochaete chrysosporium. Arch. Biochem. Biophys. 298:480-485.
    • (1992) Arch. Biochem. Biophys. , vol.298 , pp. 480-485
    • Barr, D.P.1    Shah, M.M.2    Grover, T.A.3    Aust, S.D.4
  • 5
    • 0025315157 scopus 로고
    • Oxidation of non-phenolic substrates. An expanded role for laccase in lignin biodegradation
    • Bourbonnais, R., and M. G. Paice. 1990. Oxidation of non-phenolic substrates. An expanded role for laccase in lignin biodegradation. FEBS Lett. 267:99-102.
    • (1990) FEBS Lett. , vol.267 , pp. 99-102
    • Bourbonnais, R.1    Paice, M.G.2
  • 6
    • 0024465355 scopus 로고
    • Redox and addition chemistry of quinoid compounds and its biological implications
    • Brunmark, A., and E. Cadenas. 1989. Redox and addition chemistry of quinoid compounds and its biological implications. Free Radic. Biol. Med. 7:435-477.
    • (1989) Free Radic. Biol. Med. , vol.7 , pp. 435-477
    • Brunmark, A.1    Cadenas, E.2
  • 7
    • 0018555992 scopus 로고
    • Intracellular quinone reduction in Sporotrichum pulverulentum by a NAD(P)H:Quinone oxidoreductase
    • Buswell, J. A., S. G. Hamp, and K.-E. Eriksson. 1979. Intracellular quinone reduction in Sporotrichum pulverulentum by a NAD(P)H:quinone oxidoreductase. FEBS Lett. 108:229-232.
    • (1979) FEBS Lett. , vol.108 , pp. 229-232
    • Buswell, J.A.1    Hamp, S.G.2    Eriksson, K.-E.3
  • 8
    • 4243542277 scopus 로고    scopus 로고
    • History, overview and applications of mediated lignolytic systems, especially laccase-mediator-systems (Lignozym®-process)
    • Call, H. P., and I. Mücke. 1997. History, overview and applications of mediated lignolytic systems, especially laccase-mediator-systems (Lignozym®-process). J. Biotechnol. 53:163-202.
    • (1997) J. Biotechnol. , vol.53 , pp. 163-202
    • Call, H.P.1    Mücke, I.2
  • 9
    • 0026559256 scopus 로고
    • Evidence for a new extracellular peroxidase: Manganese inhibited peroxidase from the white-rot fungus Bjerkandera sp. Bos 55
    • de Jong, E., J. A. Field, and J. A. M. Bont. 1992. Evidence for a new extracellular peroxidase: manganese inhibited peroxidase from the white-rot fungus Bjerkandera sp. Bos 55. FEBS Lett. 299:107-110.
    • (1992) FEBS Lett. , vol.299 , pp. 107-110
    • De Jong, E.1    Field, J.A.2    Bont, J.A.M.3
  • 10
    • 0030570825 scopus 로고    scopus 로고
    • A fungal metabolite mediates degradation of non-phenolic lignin structures and synthetic lignin by laccase
    • Eggert, C., U. Temp, J. F. D. Dean, and K.-E. L. Eriksson. 1996. A fungal metabolite mediates degradation of non-phenolic lignin structures and synthetic lignin by laccase. FEBS Lett. 391:144-148.
    • (1996) FEBS Lett. , vol.391 , pp. 144-148
    • Eggert, C.1    Temp, U.2    Dean, J.F.D.3    Eriksson, K.-E.L.4
  • 11
  • 12
    • 0021065373 scopus 로고
    • Relationship between lignin degradation and production of reduced oxygen species by Phanerochaete chrysosporium
    • Faison, B. D., and T. K. Kirk. 1983. Relationship between lignin degradation and production of reduced oxygen species by Phanerochaete chrysosporium. Appl. Environ. Microbiol. 46:1140-1145.
    • (1983) Appl. Environ. Microbiol. , vol.46 , pp. 1140-1145
    • Faison, B.D.1    Kirk, T.K.2
  • 13
    • 84961479354 scopus 로고
    • Wood decay by brown-rot fungi: Changes in pore structure and cell wall volume
    • Flournoy, D. S., T. K. Kirk, and T. L. Highley. 1991. Wood decay by brown-rot fungi: changes in pore structure and cell wall volume. Holzforschung 45:383-388.
    • (1991) Holzforschung , vol.45 , pp. 383-388
    • Flournoy, D.S.1    Kirk, T.K.2    Highley, T.L.3
  • 14
    • 84944300724 scopus 로고
    • Changes in the size and volume of pores in sweetgum wood during simultaneous rot by Phanerochaete chrysosporium Burds
    • Flournoy, D. S., J. A. Paul, T. K. Kirk, and T. L. Highley. 1993. Changes in the size and volume of pores in sweetgum wood during simultaneous rot by Phanerochaete chrysosporium Burds. Holzforschung 47:297-301.
    • (1993) Holzforschung , vol.47 , pp. 297-301
    • Flournoy, D.S.1    Paul, J.A.2    Kirk, T.K.3    Highley, T.L.4
  • 15
    • 84942966107 scopus 로고
    • .-) in oxidative delignification, studied with 4-t-butylsyringol and 4-t-butylguaiacol. Part I. The mechanism of aromatic ring opening
    • .-) in oxidative delignification, studied with 4-t-butylsyringol and 4-t-butylguaiacol. Part I. The mechanism of aromatic ring opening. Holzforschung 48:405-414.
    • (1994) Holzforschung , vol.48 , pp. 405-414
    • Gierer, J.1    Yang, E.Q.2    Reitberger, T.3
  • 18
    • 0026662089 scopus 로고
    • Substrate specificity and properties of the aryl-alcohol oxidase from the ligninolytic fungus Pleurotus eryngii
    • Guillén, F., A. T. Martínez, and M. J. Martínez. 1992. Substrate specificity and properties of the aryl-alcohol oxidase from the ligninolytic fungus Pleurotus eryngii. Eur. J. Biochem. 209:603-611.
    • (1992) Eur. J. Biochem. , vol.209 , pp. 603-611
    • Guillén, F.1    Martínez, A.T.2    Martínez, M.J.3
  • 19
    • 0028173943 scopus 로고
    • Hydrogen peroxide-producing system of Pleurotus eryngii involving the extracellular enzyme aryl-alcohol oxidase
    • Guillén, F., A. T. Martínez, M. J. Martínez, and C. S. Evans. 1994. Hydrogen peroxide-producing system of Pleurotus eryngii involving the extracellular enzyme aryl-alcohol oxidase. Appl. Microbiol. Biotechnol. 41:465-470.
    • (1994) Appl. Microbiol. Biotechnol. , vol.41 , pp. 465-470
    • Guillén, F.1    Martínez, A.T.2    Martínez, M.J.3    Evans, C.S.4
  • 21
    • 0031105162 scopus 로고    scopus 로고
    • Quinone redox cycling in the ligninolytic fungus Pleurotus eryngii leading to extracellular production of superoxide anion radical
    • Guillén, F., M. J. Martínez, C. Muñoz, and A. T. Martínez. 1997. Quinone redox cycling in the ligninolytic fungus Pleurotus eryngii leading to extracellular production of superoxide anion radical. Arch. Biochem. Biophys. 339: 190-199.
    • (1997) Arch. Biochem. Biophys. , vol.339 , pp. 190-199
    • Guillén, F.1    Martínez, M.J.2    Muñoz, C.3    Martínez, A.T.4
  • 22
    • 0028291491 scopus 로고
    • Anisaldehyde production and aryl-alcohol oxidase and dehydrogenase activities in ligninolytic fungi from the genus Pleurotus
    • Gutiérrez, A., L. Caramelo, A. Prieto, M. J. Martínez, and A. T. Martínez. 1994. Anisaldehyde production and aryl-alcohol oxidase and dehydrogenase activities in ligninolytic fungi from the genus Pleurotus. Appl. Environ. Microbiol. 60:1783-1788.
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 1783-1788
    • Gutiérrez, A.1    Caramelo, L.2    Prieto, A.3    Martínez, M.J.4    Martínez, A.T.5
  • 23
    • 0001615352 scopus 로고
    • Oxidation of veratryl alcohol by the lignin peroxidase of Phanerochaete chrysosporium
    • Haemmerli, S. D., H. E. Schoemaker, H. W. H. Schmidt, and M. S. A. Leisola. 1987. Oxidation of veratryl alcohol by the lignin peroxidase of Phanerochaete chrysosporium. FEBS Lett. 220:149-154.
    • (1987) FEBS Lett. , vol.220 , pp. 149-154
    • Haemmerli, S.D.1    Schoemaker, H.E.2    Schmidt, H.W.H.3    Leisola, M.S.A.4
  • 24
    • 0024654139 scopus 로고
    • Biomimetic oxidation of nonphenolic lignin models by Mn(III): New observations on the oxidizability of guaiacyl and syringyl substructures
    • Hammel, K. E., P. J. Tardone, M. A. Moen, and L. A. Price. 1989. Biomimetic oxidation of nonphenolic lignin models by Mn(III): new observations on the oxidizability of guaiacyl and syringyl substructures. Arch. Biochem. Biophys. 270:404-409.
    • (1989) Arch. Biochem. Biophys. , vol.270 , pp. 404-409
    • Hammel, K.E.1    Tardone, P.J.2    Moen, M.A.3    Price, L.A.4
  • 26
    • 0000242123 scopus 로고
    • Veratryl alcohol as a mediator and the role of radical cations in lignin biodegradation by Phanerochaete chrysosporium
    • Harvey, P. J., H. E. Schoemaker, and J. M. Palmer. 1986. Veratryl alcohol as a mediator and the role of radical cations in lignin biodegradation by Phanerochaete chrysosporium. FEBS Lett. 195:242-246.
    • (1986) FEBS Lett. , vol.195 , pp. 242-246
    • Harvey, P.J.1    Schoemaker, H.E.2    Palmer, J.M.3
  • 27
  • 28
    • 0019804120 scopus 로고
    • Toxic drug effects associated with oxygen metabolism: Redox cycling and lipid peroxidation
    • Kappus, H., and H. Sies. 1981. Toxic drug effects associated with oxygen metabolism: redox cycling and lipid peroxidation. Experientia 37:1233-1241.
    • (1981) Experientia , vol.37 , pp. 1233-1241
    • Kappus, H.1    Sies, H.2
  • 29
    • 0023264566 scopus 로고
    • 2 production by Phanerochaete chrysosporium
    • 2 production by Phanerochaete chrysosporium. J. Bacteriol. 169:2195-2201.
    • (1987) J. Bacteriol. , vol.169 , pp. 2195-2201
    • Kersten, P.J.1    Kirk, T.K.2
  • 30
    • 0023478845 scopus 로고
    • Enzymatic "combustion": The microbial degradation of lignin
    • Kirk, T. K., and R. L. Farrell. 1987. Enzymatic "combustion": the microbial degradation of lignin. Annu. Rev. Microhiol. 41:465-505.
    • (1987) Annu. Rev. Microhiol. , vol.41 , pp. 465-505
    • Kirk, T.K.1    Farrell, R.L.2
  • 31
    • 0027295913 scopus 로고
    • Glyoxylate-supported reactions catalyzed by Mn peroxidase of Phanerochaete chrysospurium: Activity in the absence of added hydrogen peroxide
    • Kuan, I. C., and M. Tien. 1993. Glyoxylate-supported reactions catalyzed by Mn peroxidase of Phanerochaete chrysospurium: activity in the absence of added hydrogen peroxide. Arch. Biochem. Biophys. 302:447-454.
    • (1993) Arch. Biochem. Biophys. , vol.302 , pp. 447-454
    • Kuan, I.C.1    Tien, M.2
  • 32
    • 0027406829 scopus 로고
    • Stimulation of Mn-peroxidase activity: A possible role for oxalate in lignin biodegradation
    • Kuan, I. C., and M. Tien. 1993. Stimulation of Mn-peroxidase activity: a possible role for oxalate in lignin biodegradation. Proc. Natl. Acad. Sci. USA 90:1242-1246.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 1242-1246
    • Kuan, I.C.1    Tien, M.2
  • 33
    • 0008203073 scopus 로고
    • The mechanism of lignin degradation
    • M. P. Coughlan (ed.). Elsevier Applied Science, London, United Kingdom
    • Leisola, M. S. A., and S. García. 1989. The mechanism of lignin degradation, p. 89-99. In M. P. Coughlan (ed.), Enzyme systems for lignocellulose degradation. Elsevier Applied Science, London, United Kingdom.
    • (1989) Enzyme Systems for Lignocellulose Degradation , pp. 89-99
    • Leisola, M.S.A.1    García, S.2
  • 34
    • 0021330759 scopus 로고
    • The effect of pH on the transformation of syringic and vanillic acids by the laccases of Rhizoctonia practicola and Trametes versicolor
    • Leonowicz, A., R. U. Edgehill, and J. M. Bollag. 1984. The effect of pH on the transformation of syringic and vanillic acids by the laccases of Rhizoctonia practicola and Trametes versicolor. Arch. Microbiol. 137:89-96.
    • (1984) Arch. Microbiol. , vol.137 , pp. 89-96
    • Leonowicz, A.1    Edgehill, R.U.2    Bollag, J.M.3
  • 36
    • 0029926079 scopus 로고    scopus 로고
    • Purification and catalytic properties of two manganese-peroxidase isoenzymes from Pleurotus eryngii
    • Martínez, M. J., F. J. Ruiz-Dueñas, F. Guillén, and A. T. Martínez. 1996. Purification and catalytic properties of two manganese-peroxidase isoenzymes from Pleurotus eryngii. Eur. J. Biochem. 237:424-432.
    • (1996) Eur. J. Biochem. , vol.237 , pp. 424-432
    • Martínez, M.J.1    Ruiz-Dueñas, F.J.2    Guillén, F.3    Martínez, A.T.4
  • 37
    • 0021813669 scopus 로고
    • Some properties of cellobiose oxidase from the white-rot fungus Sparotrichum pulverulentum
    • Morpeth, F. F. 1985. Some properties of cellobiose oxidase from the white-rot fungus Sparotrichum pulverulentum. Biochem. J. 228:557-564.
    • (1985) Biochem. J. , vol.228 , pp. 557-564
    • Morpeth, F.F.1
  • 39
    • 0025101590 scopus 로고
    • Effect of superoxide dismutase on the automation of substituted hydro- and seminaphthoquinones
    • Öllinger, K., G. D. Buffinton, L. Ernster, and E. Cadenas. 1990. Effect of superoxide dismutase on the automation of substituted hydro- and seminaphthoquinones. Chem.-Biol. Interact. 73:53-76.
    • (1990) Chem.-Biol. Interact. , vol.73 , pp. 53-76
    • Öllinger, K.1    Buffinton, G.D.2    Ernster, L.3    Cadenas, E.4
  • 40
    • 0026795829 scopus 로고
    • Thiol oxidation coupled to DT-diaphorase-catalysed reduction of diaziquione
    • Ordoñez, I. D., and E. Cadenas. 1992. Thiol oxidation coupled to DT-diaphorase-catalysed reduction of diaziquione. Biochem. J. 286:481-490.
    • (1992) Biochem. J. , vol.286 , pp. 481-490
    • Ordoñez, I.D.1    Cadenas, E.2
  • 41
    • 0025202423 scopus 로고
    • 2+ in the presence of veratryl alcohol, malonic or oxalic acid, and oxygen
    • 2+ in the presence of veratryl alcohol, malonic or oxalic acid, and oxygen. Biochemistry 29:10475-10480.
    • (1990) Biochemistry , vol.29 , pp. 10475-10480
    • Popp, J.L.1    Kalyanaraman, B.2    Kirk, T.K.3
  • 42
    • 0031991239 scopus 로고    scopus 로고
    • Fully reversible redox cycling of 2,6-dimethoxy-1,4-benzoquinone induced by ascorbate
    • Mosc.
    • Roginsky, V. A., G. Bruchelt, and H. B. Stegmann. 1998. Fully reversible redox cycling of 2,6-dimethoxy-1,4-benzoquinone induced by ascorbate. Biochemistry (Mosc.) 63:200-206.
    • (1998) Biochemistry , vol.63 , pp. 200-206
    • Roginsky, V.A.1    Bruchelt, G.2    Stegmann, H.B.3
  • 44
  • 46
    • 0008669294 scopus 로고
    • Roles of secondary metabolism of wood rotting fungi in biodegradation of lignocellulosic materials
    • N. G. Lewis and M. G. Paice (ed.). American Chemical Society, Washington, D. C.
    • Shimada, M., A. Ohta, H. Kurosaka, T. Hattori, T. Higuchi, and M. Takahashi. 1989. Roles of secondary metabolism of wood rotting fungi in biodegradation of lignocellulosic materials, p. 412-125. In N. G. Lewis and M. G. Paice (ed.), Plant cell wall polymers. American Chemical Society, Washington, D. C.
    • (1989) Plant Cell Wall Polymers , pp. 412-1125
    • Shimada, M.1    Ohta, A.2    Kurosaka, H.3    Hattori, T.4    Higuchi, T.5    Takahashi, M.6
  • 47
    • 0028013536 scopus 로고
    • The structure and function of fungal laccases
    • Read
    • Thurston, C. F. 1994. The structure and function of fungal laccases. Microbiology (Read.) 140:19-26.
    • (1994) Microbiology , vol.140 , pp. 19-26
    • Thurston, C.F.1
  • 48
    • 37049181820 scopus 로고
    • Lignin-degrading enzyme from the hymenomycete Phanerochaete chrysosporium Burds
    • Tien, M., and T. K. Kirk. 1983. Lignin-degrading enzyme from the hymenomycete Phanerochaete chrysosporium Burds. Science 221:661-663.
    • (1983) Science , vol.221 , pp. 661-663
    • Tien, M.1    Kirk, T.K.2
  • 49
    • 0031985659 scopus 로고    scopus 로고
    • Manganese peroxidase-dependent oxidation of glyoxylic and oxalic acids synthesized by Ceriporiopsis subvermispora produces extracellular hydrogen peroxide
    • Urzúa, U., P. J. Kersten, and R. Vicuña. 1998. Manganese peroxidase-dependent oxidation of glyoxylic and oxalic acids synthesized by Ceriporiopsis subvermispora produces extracellular hydrogen peroxide. Appl. Environ. Microbiol. 64:68-73.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 68-73
    • Urzúa, U.1    Kersten, P.J.2    Vicuña, R.3
  • 50
    • 0025769643 scopus 로고
    • In vitro depolymerization of lignin by manganese peroxidase of Phanerochaete chrysosporium
    • Wariishi, H., K. Valli, and M. H. Gold. 1991. In vitro depolymerization of lignin by manganese peroxidase of Phanerochaete chrysosporium. Biochem. Biophys. Res. Commun. 176:269-275.
    • (1991) Biochem. Biophys. Res. Commun. , vol.176 , pp. 269-275
    • Wariishi, H.1    Valli, K.2    Gold, M.H.3
  • 51
    • 0028211722 scopus 로고
    • Pathways of production of Fenton's reagent by woodrotting fungi
    • Wood, P. M. 1994. Pathways of production of Fenton's reagent by woodrotting fungi. FEMS Microbiol. Rev. 13:313-320.
    • (1994) FEMS Microbiol. Rev. , vol.13 , pp. 313-320
    • Wood, P.M.1


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