메뉴 건너뛰기




Volumn 98, Issue 22, 2014, Pages 9283-9294

High-yield production of manganese peroxidase, lignin peroxidase, and versatile peroxidase in Phanerochaete chrysosporium

Author keywords

Fungal transformation; Heterologous expression; Phanerochaete chrysosporium; Shock waves; Versatile peroxidase; White rot fungi

Indexed keywords

BIOTECHNOLOGY; ENZYME ACTIVITY; GENE EXPRESSION; LIGNIN; MANGANESE; METABOLISM; POLYMERASE CHAIN REACTION; SHOCK WAVES;

EID: 84925489180     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-014-6105-9     Document Type: Article
Times cited : (56)

References (47)
  • 1
    • 84873723272 scopus 로고    scopus 로고
    • Insights into lignin degradation and its potential industrial applications
    • Abdel-Hamid AM, Solbiati JO, Cann IK (2012) Insights into lignin degradation and its potential industrial applications. Adv Appl Microbiol 82:1–28
    • (2012) Adv Appl Microbiol , vol.82 , pp. 1-28
    • Abdel-Hamid, A.M.1    Solbiati, J.O.2    Cann, I.K.3
  • 2
    • 0001667936 scopus 로고
    • Mating system and basidiospore formation in the lignin-degrading basidiomycete Phanerochaete chrysosporium
    • PID: 16347375, COI: 1:CAS:528:DyaL2sXkvFegs70%3D
    • Alic M, Letzring C, Gold MH (1987) Mating system and basidiospore formation in the lignin-degrading basidiomycete Phanerochaete chrysosporium. Appl Environ Microbiol 53:1464–1469
    • (1987) Appl Environ Microbiol , vol.53 , pp. 1464-1469
    • Alic, M.1    Letzring, C.2    Gold, M.H.3
  • 3
    • 84864387203 scopus 로고    scopus 로고
    • 2 stability study of active Pleurotus eryngii versatile peroxidase in Escherichia coli
    • PID: 22566208, COI: 1:CAS:528:DC%2BC38XhtVyks7zF
    • 2 stability study of active Pleurotus eryngii versatile peroxidase in Escherichia coli. Biotechnol Lett 34:1537–1543
    • (2012) Biotechnol Lett , vol.34 , pp. 1537-1543
    • Bao, X.1    Liu, A.2    Lu, X.3    Li, J.J.4
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • PID: 942051, COI: 1:CAS:528:DyaE28XksVehtrY%3D
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248–254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0033537844 scopus 로고    scopus 로고
    • Description of a versatile peroxidase involved in the natural degradation of lignin that has both manganese peroxidase and lignin peroxidase substrate interaction sites
    • PID: 10187820, COI: 1:CAS:528:DyaK1MXis1GjtbY%3D
    • Camarero S, Sarkar S, Ruiz-Dueñas FJ, Martínez MJ, Martínez ÁT (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
    • (1999) J Biol Chem , vol.274 , pp. 10324-10330
    • Camarero, S.1    Sarkar, S.2    Ruiz-Dueñas, F.J.3    Martínez, M.J.4    Martínez, Á.T.5
  • 6
    • 0033931925 scopus 로고    scopus 로고
    • Studies on the production of fungal peroxidases in Aspergillus niger
    • PID: 10877800, COI: 1:CAS:528:DC%2BD3cXkslKlt70%3D
    • Conesa A, van den Hondel CA, Punt PJ (2000) Studies on the production of fungal peroxidases in Aspergillus niger. Appl Environ Microbiol 66:3016–3023
    • (2000) Appl Environ Microbiol , vol.66 , pp. 3016-3023
    • Conesa, A.1    van den Hondel, C.A.2    Punt, P.J.3
  • 7
    • 79952178786 scopus 로고    scopus 로고
    • Fungal biodegradation and enzymatic modification of lignin
    • PID: 21968746, COI: 1:CAS:528:DC%2BC3MXitlOrurs%3D
    • Dashtban M, Schraft H, Syed TA, Qin W (2010) Fungal biodegradation and enzymatic modification of lignin. Int J Biochem Mol Biol 1:36–50
    • (2010) Int J Biochem Mol Biol , vol.1 , pp. 36-50
    • Dashtban, M.1    Schraft, H.2    Syed, T.A.3    Qin, W.4
  • 8
    • 11144275965 scopus 로고    scopus 로고
    • Transformation of halogenated pesticides by versatile peroxidase from Bjerkandera adusta
    • COI: 1:CAS:528:DC%2BD2MXjtlOj
    • Davila-Vazquez G, Tinoco R, Pickard MA, Vazquez-Duhalt R (2005) Transformation of halogenated pesticides by versatile peroxidase from Bjerkandera adusta. Enzym Microb Technol 36:223–231
    • (2005) Enzym Microb Technol , vol.36 , pp. 223-231
    • Davila-Vazquez, G.1    Tinoco, R.2    Pickard, M.A.3    Vazquez-Duhalt, R.4
  • 9
    • 58149102783 scopus 로고    scopus 로고
    • Effect of culture temperature on the heterologous expression of Pleurotus eryngii versatile peroxidase in Aspergillus hosts
    • PID: 18481101, COI: 1:CAS:528:DC%2BD1cXhsFWrsrrE
    • Eibes GM, Lu-Chau TA, Ruiz-Dueñas FJ, Feijoo G, Martínez MJ, Martínez AT, Lema JM (2009) Effect of culture temperature on the heterologous expression of Pleurotus eryngii versatile peroxidase in Aspergillus hosts. Bioprocess Biosyst Eng 32:129–134
    • (2009) Bioprocess Biosyst Eng , vol.32 , pp. 129-134
    • Eibes, G.M.1    Lu-Chau, T.A.2    Ruiz-Dueñas, F.J.3    Feijoo, G.4    Martínez, M.J.5    Martínez, A.T.6    Lema, J.M.7
  • 10
    • 70350221628 scopus 로고    scopus 로고
    • Physiological regulation of laccase and manganese peroxidase production by white-rot Basidiomycetes
    • PID: 19559737, COI: 1:CAS:528:DC%2BD1MXhtlCntr7E
    • Elisashvili V, Kachlishvili E (2009) Physiological regulation of laccase and manganese peroxidase production by white-rot Basidiomycetes. J Biotechnol 144:37–42
    • (2009) J Biotechnol , vol.144 , pp. 37-42
    • Elisashvili, V.1    Kachlishvili, E.2
  • 11
    • 57049150206 scopus 로고    scopus 로고
    • Selection and optimization of microbial hosts for biofuels production
    • PID: 18655844, COI: 1:CAS:528:DC%2BD1cXhsVKrt7vE
    • Fischer CR, Klein-Marcuschamer D, Stephanopoulos G (2008) Selection and optimization of microbial hosts for biofuels production. Metab Eng 10:295–304
    • (2008) Metab Eng , vol.10 , pp. 295-304
    • Fischer, C.R.1    Klein-Marcuschamer, D.2    Stephanopoulos, G.3
  • 12
    • 84055213590 scopus 로고    scopus 로고
    • Directed evolution of a temperature-, peroxide-and alkaline pH-tolerant versatile peroxidase
    • PID: 21980920, COI: 1:CAS:528:DC%2BC3MXhs1CgsL%2FP
    • Garcia-Ruiz E, Gonzalez-Perez D, Ruiz-Dueñas FJ, Martínez AT, Alcalde M (2012) Directed evolution of a temperature-, peroxide-and alkaline pH-tolerant versatile peroxidase. Biochem J 441:487–498
    • (2012) Biochem J , vol.441 , pp. 487-498
    • Garcia-Ruiz, E.1    Gonzalez-Perez, D.2    Ruiz-Dueñas, F.J.3    Martínez, A.T.4    Alcalde, M.5
  • 13
    • 0031890797 scopus 로고    scopus 로고
    • Reverse transcription-PCR analysis of the regulation of the manganese peroxidase gene family
    • PID: 9464395, COI: 1:CAS:528:DyaK1cXpsVSrtA%3D%3D
    • Gettemy JM, Ma B, Alic M, Gold MH (1998) Reverse transcription-PCR analysis of the regulation of the manganese peroxidase gene family. Appl Environ Microbiol 64:569–574
    • (1998) Appl Environ Microbiol , vol.64 , pp. 569-574
    • Gettemy, J.M.1    Ma, B.2    Alic, M.3    Gold, M.H.4
  • 14
    • 0026440132 scopus 로고
    • Sequence analysis of the glyceraldehyde-3-phosphate dehydrogenase genes from the basidiomycetes Schizophyllum commune, Phanerochaete chrysosporium and Agaricus bisporus
    • PID: 1473176, COI: 1:CAS:528:DyaK3sXlvFKrtb4%3D
    • Harmsen MC, Schuren FHJ, Moukha SM, van Zuilen CM, Punt PJ, Wessels JGH (1992) Sequence analysis of the glyceraldehyde-3-phosphate dehydrogenase genes from the basidiomycetes Schizophyllum commune, Phanerochaete chrysosporium and Agaricus bisporus. Curr Genet 22:447–454
    • (1992) Curr Genet , vol.22 , pp. 447-454
    • Harmsen, M.C.1    Schuren, F.H.J.2    Moukha, S.M.3    van Zuilen, C.M.4    Punt, P.J.5    Wessels, J.G.H.6
  • 15
    • 0032577520 scopus 로고    scopus 로고
    • A study on reducing substrates of manganese-oxidizing peroxidases from Pleurotus eryngii and Bjerkandera adusta
    • Heinfling A, Ruiz-Dueñas FJ, Martínez MJ, Bergbauer M, Szewzyk U, Martínez AT (1998) A study on reducing substrates of manganese-oxidizing peroxidases from Pleurotus eryngii and Bjerkandera adusta. FEBS Lett 428:141–146
    • (1998) FEBS Lett , vol.428 , pp. 141-146
    • Heinfling, A.1    Ruiz-Dueñas, F.J.2    Martínez, M.J.3    Bergbauer, M.4    Szewzyk, U.5    Martínez, A.T.6
  • 16
    • 0035010837 scopus 로고    scopus 로고
    • Homologous expression of recombinant manganese peroxidase genes in ligninolytic fungus Pleurotus ostreatus
    • PID: 11414322, COI: 1:CAS:528:DC%2BD3MXksFCrsb8%3D
    • Irie T, Honda Y, Watanabe T, Kuwahara M (2001) Homologous expression of recombinant manganese peroxidase genes in ligninolytic fungus Pleurotus ostreatus. Appl Microbiol Biotechnol 55:566–570
    • (2001) Appl Microbiol Biotechnol , vol.55 , pp. 566-570
    • Irie, T.1    Honda, Y.2    Watanabe, T.3    Kuwahara, M.4
  • 17
    • 84870348809 scopus 로고    scopus 로고
    • Fungal laccase, manganese peroxidase and lignin peroxidase: gene expression and regulation
    • COI: 1:CAS:528:DC%2BC38Xhs1ShtrbK
    • Janusz G, Kucharzyk KH, Pawlik A, Staszczak M, Paszczynski AJ (2013) Fungal laccase, manganese peroxidase and lignin peroxidase: gene expression and regulation. Enzym Microb Technol 52:1–12
    • (2013) Enzym Microb Technol , vol.52 , pp. 1-12
    • Janusz, G.1    Kucharzyk, K.H.2    Pawlik, A.3    Staszczak, M.4    Paszczynski, A.J.5
  • 18
    • 38449100406 scopus 로고    scopus 로고
    • Production and separation of manganese peroxidase from heme amended yeast cultures
    • PID: 17680655, COI: 1:CAS:528:DC%2BD1cXns1SqtA%3D%3D
    • Jiang F, Kongsaeree P, Charron R, Lajoie C, Xu H, Scott G, Kelly C (2008) Production and separation of manganese peroxidase from heme amended yeast cultures. Biotechnol Bioeng 99:540–549
    • (2008) Biotechnol Bioeng , vol.99 , pp. 540-549
    • Jiang, F.1    Kongsaeree, P.2    Charron, R.3    Lajoie, C.4    Xu, H.5    Scott, G.6    Kelly, C.7
  • 19
    • 0026348456 scopus 로고
    • Heterologous expression and characterization of an active lignin peroxidase from Phanerochaete chrysosporium using recombinant baculovirus
    • PID: 1952950, COI: 1:CAS:528:DyaK38XlsVWrsw%3D%3D
    • Johnson TM, Li JKK (1991) Heterologous expression and characterization of an active lignin peroxidase from Phanerochaete chrysosporium using recombinant baculovirus. Arch Biochem Biophys 291:371–378
    • (1991) Arch Biochem Biophys , vol.291 , pp. 371-378
    • Johnson, T.M.1    Li, J.K.K.2
  • 20
    • 0012474874 scopus 로고    scopus 로고
    • Fundamentals of growth, storage, genetics and microscopy of Aspergillus nidulans
    • Kaminskyj SGW (2001) Fundamentals of growth, storage, genetics and microscopy of Aspergillus nidulans. Fungal Genet Newsl 48:25–31
    • (2001) Fungal Genet Newsl , vol.48 , pp. 25-31
    • Kaminskyj, S.G.W.1
  • 21
    • 14844323717 scopus 로고    scopus 로고
    • Direct oxidation of polymeric substrates by multifunctional manganese peroxidase isoenzyme from Pleurotus ostreatus without redox mediators
    • PID: 15461584, COI: 1:CAS:528:DC%2BD2MXhsFSmtr4%3D
    • Kamitsuji H, Watanabe T, Honda Y, Kuwahara M (2005) Direct oxidation of polymeric substrates by multifunctional manganese peroxidase isoenzyme from Pleurotus ostreatus without redox mediators. Biochem J 386:387–93
    • (2005) Biochem J , vol.386 , pp. 387-393
    • Kamitsuji, H.1    Watanabe, T.2    Honda, Y.3    Kuwahara, M.4
  • 23
    • 84905006343 scopus 로고    scopus 로고
    • 2+-deficiency reveals a key role for the Pleurotus ostreatus versatile peroxidase (VP4) in oxidation of aromatic compounds
    • PID: 24737058, COI: 1:CAS:528:DC%2BC2cXmsVChsrc%3D
    • 2+-deficiency reveals a key role for the Pleurotus ostreatus versatile peroxidase (VP4) in oxidation of aromatic compounds. Appl Microbiol Biotechnol 98:6795–6804
    • (2014) Appl Microbiol Biotechnol , vol.98 , pp. 6795-6804
    • Knop, D.1    Ben-Ari, J.2    Salame, T.M.3    Levinson, D.4    Yarden, O.5    Hadar, Y.6
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of head of bacteriophage T4
    • PID: 5432063, COI: 1:CAS:528:DC%2BD3MXlsFags7s%3D
    • Laemmli UK (1970) Cleavage of structural proteins during assembly of head of bacteriophage T4. Nature 227:680–685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 0141631799 scopus 로고    scopus 로고
    • Homologous expression of Phanerochaete chrysosporium manganese peroxidase, using bialaphos resistance as a dominant selectable marker
    • PID: 12844234, COI: 1:CAS:528:DC%2BD3sXmslSis7o%3D
    • Ma B, Mayfield MB, Gold MH (2003) Homologous expression of Phanerochaete chrysosporium manganese peroxidase, using bialaphos resistance as a dominant selectable marker. Curr Genet 43:407–414
    • (2003) Curr Genet , vol.43 , pp. 407-414
    • Ma, B.1    Mayfield, M.B.2    Gold, M.H.3
  • 27
    • 0029926079 scopus 로고    scopus 로고
    • Purification and catalytic properties of two manganese peroxidase isoenzymes from Pleurotus eryngii
    • PID: 8647081
    • Martínez MJ, Ruiz-Dueñas FJ, Guillén F, Martínez ÁT (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, Á.T.4
  • 29
    • 0028139313 scopus 로고
    • Homologous expression of recombinant manganese peroxidase in Phanerochaete chrysosporium
    • PID: 7811070, COI: 1:STN:280:DyaK2M7htVWhsA%3D%3D
    • Mayfield MB, Kishi K, Alic M, Gold MH (1994) Homologous expression of recombinant manganese peroxidase in Phanerochaete chrysosporium. Appl Environ Microbiol 60:4303–4309
    • (1994) Appl Environ Microbiol , vol.60 , pp. 4303-4309
    • Mayfield, M.B.1    Kishi, K.2    Alic, M.3    Gold, M.H.4
  • 30
    • 38349002470 scopus 로고    scopus 로고
    • Genetic engineering of filamentous fungi—progress, obstacles and future trends
    • PID: 18201856, COI: 1:CAS:528:DC%2BD1cXptlSmtQ%3D%3D
    • Meyer V (2008) Genetic engineering of filamentous fungi—progress, obstacles and future trends. Biotechnol Adv 26:177–185
    • (2008) Biotechnol Adv , vol.26 , pp. 177-185
    • Meyer, V.1
  • 32
    • 33947543926 scopus 로고    scopus 로고
    • Lignin transformation by a versatile peroxidase from a novel Bjerkandera sp. strain
    • COI: 1:CAS:528:DC%2BD2sXjslGmsLY%3D
    • Moreira PR, Almeida-Vara E, Malcata FX, Duarte JC (2007) Lignin transformation by a versatile peroxidase from a novel Bjerkandera sp. strain. Int Biodeter Biodegr 59:234–238
    • (2007) Int Biodeter Biodegr , vol.59 , pp. 234-238
    • Moreira, P.R.1    Almeida-Vara, E.2    Malcata, F.X.3    Duarte, J.C.4
  • 33
    • 77953022341 scopus 로고    scopus 로고
    • A comparative view of metabolite and substrate stress and tolerance in microbial bioprocessing: from biofuels and chemicals, to biocatalysis and bioremediation
    • PID: 20346409, COI: 1:CAS:528:DC%2BC3cXntVegsLc%3D
    • Nicolaou SA, Gaida SM, Papoutsakis ET (2010) A comparative view of metabolite and substrate stress and tolerance in microbial bioprocessing: from biofuels and chemicals, to biocatalysis and bioremediation. Metab Eng 12:307–331
    • (2010) Metab Eng , vol.12 , pp. 307-331
    • Nicolaou, S.A.1    Gaida, S.M.2    Papoutsakis, E.T.3
  • 34
    • 0342514587 scopus 로고    scopus 로고
    • Different fungal manganese-oxidizing peroxidases: a comparison between Bjerkandera sp. and Phanerochaete chrysosporium
    • PID: 10682282, COI: 1:CAS:528:DC%2BD3cXmtVKgug%3D%3D
    • Palma C, Martínez AT, Lema JM, Martínez MJ (2000) Different fungal manganese-oxidizing peroxidases: a comparison between Bjerkandera sp. and Phanerochaete chrysosporium. J Biotechnol 77:235–245
    • (2000) J Biotechnol , vol.77 , pp. 235-245
    • Palma, C.1    Martínez, A.T.2    Lema, J.M.3    Martínez, M.J.4
  • 39
    • 84891627113 scopus 로고    scopus 로고
    • Inactivation of a Pleurotus ostreatus versatile peroxidase-encoding gene (mnp2) results in reduced lignin degradation
    • PID: 24119015, COI: 1:CAS:528:DC%2BC2cXlsFymtA%3D%3D
    • Salame TM, Knop D, Levinson D, Mabjeesh SJ, Yarden O, Hadar Y (2014) Inactivation of a Pleurotus ostreatus versatile peroxidase-encoding gene (mnp2) results in reduced lignin degradation. Environ Microbiol 16:265–77
    • (2014) Environ Microbiol , vol.16 , pp. 265-277
    • Salame, T.M.1    Knop, D.2    Levinson, D.3    Mabjeesh, S.J.4    Yarden, O.5    Hadar, Y.6
  • 41
    • 56349109393 scopus 로고    scopus 로고
    • The white-rot fungus Phanerochaete chrysosporium: conditions for the production of lignin-degrading enzymes
    • PID: 18810426, COI: 1:CAS:528:DC%2BD1cXhtlyjt77I
    • Singh D, Chen S (2008) The white-rot fungus Phanerochaete chrysosporium: conditions for the production of lignin-degrading enzymes. Appl Microbiol Biotechnol 81:399–417
    • (2008) Appl Microbiol Biotechnol , vol.81 , pp. 399-417
    • Singh, D.1    Chen, S.2
  • 42
    • 0032914591 scopus 로고    scopus 로고
    • Homologous expression of recombinant lignin peroxidase in Phanerochaete chrysosporium
    • PID: 10103266, COI: 1:CAS:528:DyaK1MXitlartbw%3D
    • Sollewijn Gelpke MD, Mayfield-Gambill M, Lin Cereghino GP, Gold MH (1999) Homologous expression of recombinant lignin peroxidase in Phanerochaete chrysosporium. Appl Environ Microbiol 65:1670–1674
    • (1999) Appl Environ Microbiol , vol.65 , pp. 1670-1674
    • Sollewijn Gelpke, M.D.1    Mayfield-Gambill, M.2    Lin Cereghino, G.P.3    Gold, M.H.4
  • 43
    • 0026764236 scopus 로고
    • Lignin peroxidase gene family of Phanerochaete chrysosporium: complex regulation by carbon and nitrogen limitation and identification of a second dimorphic chromosome
    • PID: 1629160, COI: 1:CAS:528:DyaK38XlsVCksrY%3D
    • Stewart P, Kersten P, Vanden Wymelenberg A, Gaskell J, Cullen D (1992) Lignin peroxidase gene family of Phanerochaete chrysosporium: complex regulation by carbon and nitrogen limitation and identification of a second dimorphic chromosome. J Bacteriol 174:5036–5042
    • (1992) J Bacteriol , vol.174 , pp. 5036-5042
    • Stewart, P.1    Kersten, P.2    Vanden Wymelenberg, A.3    Gaskell, J.4    Cullen, D.5
  • 44
    • 69749084914 scopus 로고
    • Lignin peroxidase of Phanerochaete chrysosporium
    • COI: 1:CAS:528:DyaL1MXhs1yqtbo%3D
    • Tien M, Kirk T (1988) Lignin peroxidase of Phanerochaete chrysosporium. Methods Enzymol 161:238–249
    • (1988) Methods Enzymol , vol.161 , pp. 238-249
    • Tien, M.1    Kirk, T.2
  • 45
    • 55049127293 scopus 로고    scopus 로고
    • Codon optimization increases steady-state mRNA levels in Aspergillus oryzae heterologous gene expression
    • PID: 18791013, COI: 1:CAS:528:DC%2BD1cXhtlKms7zE
    • Tokuoka M, Tanaka M, Ono K, Takagi S, Shintani T, Gomi K (2008) Codon optimization increases steady-state mRNA levels in Aspergillus oryzae heterologous gene expression. Appl Environ Microbiol 74:6538–6546
    • (2008) Appl Environ Microbiol , vol.74 , pp. 6538-6546
    • Tokuoka, M.1    Tanaka, M.2    Ono, K.3    Takagi, S.4    Shintani, T.5    Gomi, K.6
  • 46
    • 33750322286 scopus 로고    scopus 로고
    • Exclusive overproduction of recombinant versatile peroxidase MnP2 by genetically modified white rot fungus, Pleurotus ostreatus
    • PID: 16820241, COI: 1:CAS:528:DC%2BD28XhtFeqt7fI
    • Tsukihara T, Honda Y, Sakai R, Watanabe T, Watanabe T (2006) Exclusive overproduction of recombinant versatile peroxidase MnP2 by genetically modified white rot fungus, Pleurotus ostreatus. J Biotechnol 126:431–439
    • (2006) J Biotechnol , vol.126 , pp. 431-439
    • Tsukihara, T.1    Honda, Y.2    Sakai, R.3    Watanabe, T.4    Watanabe, T.5
  • 47
    • 0027096634 scopus 로고
    • Manganese (II) oxidation by manganese peroxidase from the basidiomycete Phanerochaete chrysosporium. Kinetic mechanism and role of chelators
    • PID: 1429709, COI: 1:CAS:528:DyaK38XmtVOrt74%3D
    • Wariishi H, Valli K, Gold MH (1992) Manganese (II) oxidation by manganese peroxidase from the basidiomycete Phanerochaete chrysosporium. Kinetic mechanism and role of chelators. J Biol Chem 267:23688–23695
    • (1992) J Biol Chem , vol.267 , pp. 23688-23695
    • Wariishi, H.1    Valli, K.2    Gold, M.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.