메뉴 건너뛰기




Volumn 94, Issue 3, 2012, Pages 673-683

Eukaryotic extracellular catalase-peroxidase from Magnaporthe grisea - Biophysical/chemical characterization of the first representative from a novel phytopathogenic KatG group

Author keywords

Extracellular catalase peroxidase; Oxidative stress; Peroxidases catalase superfamily; Phytopathogen; Reduction potential; Resonance Raman spectroscopy

Indexed keywords

CATALASE; CYANIDE; HISTIDINE; IMIDAZOLE DERIVATIVE; KATG PROTEIN; PEROXIDASE; PROTEIN KATG2; UNCLASSIFIED DRUG;

EID: 84857060979     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2011.09.020     Document Type: Article
Times cited : (30)

References (60)
  • 1
    • 34247111250 scopus 로고    scopus 로고
    • Prokaryotic origins of the non-animal peroxidase superfamily and organelle-mediated transmission to eukaryotes
    • DOI 10.1016/j.ygeno.2007.01.006, PII S0888754307000110
    • F. Passardi, N. Bakalovic, F.K. Teixeira, M. Margis-Pinheiro, C. Penel, and C. Dunand Prokaryotic origins of the non-animal peroxidase superfamily and organelle mediated transmission to eukaryotes Genomics 89 2007 567 579 (Pubitemid 46589946)
    • (2007) Genomics , vol.89 , Issue.5 , pp. 567-579
    • Passardi, F.1    Bakalovic, N.2    Teixeira, F.K.3    Margis-Pinheiro, M.4    Penel, C.5    Dunand, C.6
  • 3
    • 12944305786 scopus 로고
    • Superfamily of plant, fungal and bacterial peroxidases
    • K.G. Welinder Superfamily of plant, fungal and bacterial peroxidases Curr. Opin. Struct. Biol. 2 1992 388 393
    • (1992) Curr. Opin. Struct. Biol. , vol.2 , pp. 388-393
    • Welinder, K.G.1
  • 4
    • 77954283889 scopus 로고    scopus 로고
    • Heme peroxidase biochemistry - Facts and perspectives
    • C. Obinger Heme peroxidase biochemistry - facts and perspectives Arch. Biochem. Biophys. 500 2010 1 2
    • (2010) Arch. Biochem. Biophys. , vol.500 , pp. 1-2
    • Obinger, C.1
  • 5
    • 84895294751 scopus 로고    scopus 로고
    • Molecular phylogeny of heme peroxidases
    • E. Torres, M. Ayala, Springer Berlin
    • M. Zamocky, and C. Obinger Molecular phylogeny of heme peroxidases E. Torres, M. Ayala, Biocatalysis Based on Heme Peroxidases 2010 Springer Berlin 7 35
    • (2010) Biocatalysis Based on Heme Peroxidases , pp. 7-35
    • Zamocky, M.1    Obinger, C.2
  • 6
    • 34250806036 scopus 로고    scopus 로고
    • Phylogenetic distribution of catalase-peroxidases: Are there patches of order in chaos?
    • DOI 10.1016/j.gene.2007.04.016, PII S0378111907001928
    • F. Passardi, J. Favet, M. Zamocky, C. Jakopitsch, C. Penel, C. Obinger, and C. Dunand Phylogenetic distribution of catalase-peroxidases: are there patches of order in chaos? Gene 397 2007 101 113 (Pubitemid 46977137)
    • (2007) Gene , vol.397 , Issue.1-2 , pp. 101-113
    • Passardi, F.1    Zamocky, M.2    Favet, J.3    Jakopitsch, C.4    Penel, C.5    Obinger, C.6    Dunand, C.7
  • 8
    • 61449110166 scopus 로고    scopus 로고
    • Intracellular catalase/peroxidase from the phytopathogenic rice blast fungus Magnaporthe grisea: Expression analysis and biochemical characterization of the recombinant protein
    • M. Zamocky, P.G. Furtmüller, M. Bellei, G. Battistuzzi, J. Stadlmann, J. Vlasits, and C. Obinger Intracellular catalase/peroxidase from the phytopathogenic rice blast fungus Magnaporthe grisea: expression analysis and biochemical characterization of the recombinant protein Biochem. J. 418 2009 443 451
    • (2009) Biochem. J. , vol.418 , pp. 443-451
    • Zamocky, M.1    Furtmüller, P.G.2    Bellei, M.3    Battistuzzi, G.4    Stadlmann, J.5    Vlasits, J.6    Obinger, C.7
  • 10
    • 70349095242 scopus 로고    scopus 로고
    • 2 in rice cells inoculated with rice blas fungus, Magnaporthe oryzae
    • 2 in rice cells inoculated with rice blas fungus, Magnaporthe oryzae Physiologia Plantarum 137 2009 148 154
    • (2009) Physiologia Plantarum , vol.137 , pp. 148-154
    • Tanabe, S.1    Nishizawa, Y.2    Minami, E.3
  • 11
    • 33645865262 scopus 로고    scopus 로고
    • Probing the structure and bifunctionality of catalase-peroxidase (KatG)
    • G. Smulevich, E. Droghetti, C. Jakopitsch, and C. Obinger Probing the structure and bifunctionality of catalase-peroxidase (KatG) J. Inorg. Biochem. 100 2006 568 585
    • (2006) J. Inorg. Biochem. , vol.100 , pp. 568-585
    • Smulevich, G.1    Droghetti, E.2    Jakopitsch, C.3    Obinger, C.4
  • 14
    • 77956689689 scopus 로고    scopus 로고
    • Probing the two-domain structure of homodimeric prokaryotic and eukaryotic catalase-peroxidases
    • S. Banerjee, M. Zamocky, P.G. Furtmüller, and C. Obinger Probing the two-domain structure of homodimeric prokaryotic and eukaryotic catalase-peroxidases Biochim. Biophys. Acta 1804 2010 2136 2145
    • (2010) Biochim. Biophys. Acta , vol.1804 , pp. 2136-2145
    • Banerjee, S.1    Zamocky, M.2    Furtmüller, P.G.3    Obinger, C.4
  • 15
    • 0019414485 scopus 로고
    • Procedures and conditions for application of the pyridine hemochrome method to photosynthetically grown cells of Rhodopseudomonas sphaeroides
    • S. Takaichi, and S. Morita Procedures and conditions for application of the pyridine hemochrome method to photosynthetically grown cells of Rhodopseudomonas sphaeroides J. Biochem. 89 1981 1513 1519 (Pubitemid 11086516)
    • (1981) Journal of Biochemistry , vol.89 , Issue.5 , pp. 1513-1519
    • Takaichi, S.1    Morita, S.2
  • 16
    • 33747855587 scopus 로고    scopus 로고
    • A reference database for circular dichroism spectroscopy covering fold and secondary structure space
    • DOI 10.1093/bioinformatics/btl327
    • J.G. Lees, A.J. Miles, F. Wien, and B.A. Wallace A reference database for circular dichroism spectroscopy covering fold and secondary structure space Bioinformatics 22 2006 1955 1962 (Pubitemid 44283007)
    • (2006) Bioinformatics , vol.22 , Issue.16 , pp. 1955-1962
    • Lees, J.G.1    Miles, A.J.2    Wien, F.3    Wallace, B.A.4
  • 17
    • 3242877618 scopus 로고    scopus 로고
    • DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data
    • DOI 10.1093/nar/gkh371
    • L. Whitmore, and B.A. Wallace DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data Nucl. Acids Res. 32 2004 W668 W673 (Pubitemid 38997420)
    • (2004) Nucleic Acids Research , vol.32
    • Whitmore, L.1    Wallace, B.A.2
  • 18
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • L.J. McGuffin, K. Bryson, and D.T. Jones The PSIPRED protein structure prediction server Bioinformatics 16 2000 404 405 (Pubitemid 30417087)
    • (2000) Bioinformatics , vol.16 , Issue.4 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 21
    • 33645944671 scopus 로고    scopus 로고
    • Redox thermodynamics of the ferric-ferrous couple of wild-type Synechocystis KatG and KatG(Y249F)
    • M. Bellei, C. Jakopitsch, G. Battistuzzi, M. Sola, and C. Obinger Redox thermodynamics of the ferric-ferrous couple of wild-type Synechocystis KatG and KatG(Y249F) Biochemistry 45 2006 4678 4774
    • (2006) Biochemistry , vol.45 , pp. 4678-4774
    • Bellei, M.1    Jakopitsch, C.2    Battistuzzi, G.3    Sola, M.4    Obinger, C.5
  • 23
    • 0028233559 scopus 로고
    • Assays for the chlorination activity of myeloperoxidase
    • DOI 10.1016/S0076-6879(94)33056-5
    • A.J. Kettle, and C.C. Winterbourn Assays for the chlorination activity of myeloperoxidase Methods Enzymol. 233 1994 502 512 (Pubitemid 24177576)
    • (1994) Methods in Enzymology , vol.233 , pp. 502-512
    • Kettle, A.J.1    Winterbourn, C.C.2
  • 24
    • 46449120551 scopus 로고    scopus 로고
    • Fungal catalase-peroxidases - A novel group of bifunctional oxidoreductases
    • M. Zamocky, C. Jakopitsch, J. Vlasits, and C. Obinger Fungal catalase-peroxidases - a novel group of bifunctional oxidoreductases J. Biol. Inorg. Chem. 12 2007 S97
    • (2007) J. Biol. Inorg. Chem. , vol.12 , pp. 97
    • Zamocky, M.1    Jakopitsch, C.2    Vlasits, J.3    Obinger, C.4
  • 25
    • 77949431328 scopus 로고    scopus 로고
    • Identification and analysis of in planta expressed genes of Magnaporthe oryzae
    • S. Kim, J. Park, S.Y. Park, T.K. Mitchell, and Y.H. Lee Identification and analysis of in planta expressed genes of Magnaporthe oryzae BMC Genomics 11 2010 104
    • (2010) BMC Genomics , vol.11 , pp. 104
    • Kim, S.1    Park, J.2    Park, S.Y.3    Mitchell, T.K.4    Lee, Y.H.5
  • 26
    • 0036727326 scopus 로고    scopus 로고
    • Messenger RNA decay during aging and development
    • DOI 10.1016/S1568-1637(02)00023-5, PII S1568163702000235
    • G. Brewer Messenger RNA decay during aging and development Ageing Res. Rev. 1 2002 607 625 (Pubitemid 38340320)
    • (2002) Ageing Research Reviews , vol.1 , Issue.4 , pp. 607-625
    • Brewer, G.1
  • 27
    • 0345426301 scopus 로고    scopus 로고
    • Catalase-peroxidase from the cyanobacterium synechocystis PCC 6803: Cloning, overexpression in Escherichia coli, and kinetic characterization
    • DOI 10.1515/BC.1999.135
    • C. Jakopitsch, F. Rueker, G. Regelsberger, M. Dockal, G.A. Peschek, and C. Obinger Catalase-peroxidase from the cyanobacterium Synechocystis PCC 6803: cloning, overexpression in Escherichia coli, and kinetic characterization Biol. Chem. 380 1999 1087 1096 (Pubitemid 29484032)
    • (1999) Biological Chemistry , vol.380 , Issue.9 , pp. 1087-1096
    • Jakopitsch, C.1    Ruker, F.2    Regelsberger, G.3    Dockal, M.4    Peschek, G.A.5    Obinger, C.6
  • 28
    • 27944490007 scopus 로고    scopus 로고
    • Role of the Met-Tyr-Trp cross-link in Mycobacterium tuberculosis catalase-peroxidase (KatG) as revealed by KatG(M255I)
    • DOI 10.1021/bi051463q
    • R.A. Ghiladi, K.F. Medzihradszky, and P.R. Ortiz de Montellano Role of the Met-Tyr-Trp cross-link in Mycobacterium tuberculosis catalase-peroxidase (KatG) as revealed by KatG(M255I) Biochemistry 44 2005 15093 15105 (Pubitemid 41681445)
    • (2005) Biochemistry , vol.44 , Issue.46 , pp. 15093-15105
    • Ghiladi, R.A.1    Medzihradszky, K.F.2    Ortiz De Montellano, P.R.3
  • 29
    • 0037827700 scopus 로고    scopus 로고
    • Total conversion of bifunctional catalase-peroxidase (KatG) to monofunctional peroxidase by exchange of a conserved distal side tyrosine
    • DOI 10.1074/jbc.M211625200
    • C. Jakopitsch, M. Auer, A. Ivancich, F. Rueker, P.G. Furtmüller, and C. Obinger Total conversion of bifunctional catalase-peroxidase (KatG) to monofunctional peroxidase by exchange of a conserved distal side tyrosine J. Biol. Chem. 278 2003 20185 20191 (Pubitemid 36799214)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.22 , pp. 20185-20191
    • Jakopitsch, C.1    Auer, M.2    Ivancich, A.3    Ruker, F.4    Furtmuller, P.G.5    Obinger, C.6
  • 30
    • 0141761116 scopus 로고    scopus 로고
    • Distal side tryptophan, tyrosine and methionine in catalase-peroxidases are covalently linked in solution
    • DOI 10.1016/S0014-5793(03)00901-3
    • C. Jakopitsch, D. Kolarich, G. Petutschnig, P.G. Furtmüller, and C. Obinger Distal side tryptophan, tyrosine and methionine in catalase-peroxidases are covalently linked in solution FEBS Lett. 552 2003 135 140 (Pubitemid 37186849)
    • (2003) FEBS Letters , vol.552 , Issue.2-3 , pp. 135-140
    • Jakopitsch, C.1    Kolarich, D.2    Petutschnig, G.3    Furtmuller, P.G.4    Obinger, C.5
  • 31
    • 2842546487 scopus 로고
    • Structural correlations and vinyl influences in resonance Raman spectra of protoheme complexes and proteins
    • S. Choi, T.G. Spiro, K.G. Langry, K.M. Smith, D.L. Budd, and G.N. LaMar Structural correlations and vinyl influences in resonance Raman spectra of protoheme complexes and proteins J. Am. Chem. Soc. 104 1982 4345 4351
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 4345-4351
    • Choi, S.1    Spiro, T.G.2    Langry, K.G.3    Smith, K.M.4    Budd, D.L.5    Lamar, G.N.6
  • 32
    • 0242386453 scopus 로고    scopus 로고
    • Relationship between heme vinyl conformation and the protein matrix in peroxidases
    • M.P. Marzocchi, and G. Smulevich Relationship between heme vinyl conformation and the protein matrix in peroxidases J. Raman Spectros. 34 2003 725 736
    • (2003) J. Raman Spectros. , vol.34 , pp. 725-736
    • Marzocchi, M.P.1    Smulevich, G.2
  • 33
    • 0037162410 scopus 로고    scopus 로고
    • New insights into the heme cavity structure of catalase-peroxidase: A spectroscopic approach to the recombinant Synechocystis enzyme and selected distal cavity mutants
    • DOI 10.1021/bi025740u
    • H.A. Heering, C. Indiani, G. Regelsberger, C. Jakopitsch, C. Obinger, and G. Smulevich New insights into the heme cavity structure of catalase-peroxidase: a spectroscopic approach to the recombinant synechocystis enzyme and selected distal cavity mutants Biochemistry 41 2002 9237 9247 (Pubitemid 34787282)
    • (2002) Biochemistry , vol.41 , Issue.29 , pp. 9237-9247
    • Heering, H.A.1    Indiani, C.2    Regelsberger, G.3    Jakopitsch, C.4    Obinger, C.5    Smulevich, G.6
  • 34
    • 18444392102 scopus 로고    scopus 로고
    • Non-planar heme deformations and excited state displacements in horseradish peroxidase detected by Raman spectroscopy at Soret excitation
    • DOI 10.1002/jrs.1326
    • Q. Huang, and R. Schweitzer-Stenner Non-planar heme deformations and excited state displacements in horseradish peroxidase detected by Raman spectroscopy at Soret excitation J. Raman Spectros. 36 2005 363 375 (Pubitemid 40653534)
    • (2005) Journal of Raman Spectroscopy , vol.36 , Issue.4 , pp. 363-375
    • Huang, Q.1    Schweitzer-Stenner, R.2
  • 35
    • 0030467166 scopus 로고    scopus 로고
    • Assignment of protoheme Resonance Raman spectrum by heme labeling in myoglobin
    • DOI 10.1021/ja962239e, PII S0002786396022391
    • S. Hu, K.M. Smith, and T.G. Spiro Assignment of protoheme resonance Raman spectrum by heme labeling in myoglobin J. Am. Chem. Soc. 118 1996 12638 12646 (Pubitemid 27041986)
    • (1996) Journal of the American Chemical Society , vol.118 , Issue.50 , pp. 12638-12646
    • Hu, S.1    Smith, K.M.2    Spiro, T.G.3
  • 36
    • 0027818118 scopus 로고
    • Complete assignment of cytochrome c resonance Raman spectra via enzymatic reconstitution with isotopically labeled hemes
    • S. Hu, I.K. Morris, J.P. Singh, K.M. Smith, and T.G. Spiro Complete assignment of cytochrome c resonance Raman spectra via enzymatic reconstitution with isotopically labeled hemes J. Am. Chem. Soc. 115 1993 12446 12458 (Pubitemid 24078345)
    • (1993) Journal of the American Chemical Society , vol.115 , Issue.26 , pp. 12446-12458
    • Hu, S.1    Morris, I.K.2    Singh, J.P.3    Smith, K.M.4    Spiro, T.G.5
  • 39
    • 0034596337 scopus 로고    scopus 로고
    • Benzohydroxamic acid - peroxidase complexes: Spectroscopic characterization of a novel heme spin species
    • DOI 10.1021/ja000587h
    • C. Indiani, A. Feis, B.D. Howes, M.P. Marzocchi, and G. Smulevich Benzohydroxamic acid-peroxidase complexes: spectroscopic characterization of a novel heme spin species J. Am. Chem. Soc. 122 2000 7368 7376 (Pubitemid 30636725)
    • (2000) Journal of the American Chemical Society , vol.122 , Issue.30 , pp. 7368-7376
    • Indiani, C.1    Feis, A.2    Howes, B.D.3    Marzocchi, M.P.4    Smulevich, G.5
  • 40
    • 20444466524 scopus 로고    scopus 로고
    • Fifteen years of Raman spectroscopy of engineered heme containing peroxidases: What have we learned?
    • DOI 10.1021/ar020112q
    • G. Smulevich, A. Feis, and B.D. Howes Fifteen years of Raman spectroscopy of engineered heme containing peroxidases: what have we learned? Acc. Chem. Res. 38 2005 433 440 (Pubitemid 40816655)
    • (2005) Accounts of Chemical Research , vol.38 , Issue.5 , pp. 433-440
    • Smulevich, G.1    Feis, A.2    Howes, B.D.3
  • 41
    • 77956900727 scopus 로고    scopus 로고
    • Structure-function relationships among heme peroxidases: New insights from electronic absorption, resonance Raman and multifrequence electron paramagnetic resonance spectroscopies
    • K.M. Kadish, K.M. Smith, R. Guilard, World Scientific Singapore
    • G. Smulevich, A. Feis, B.D. Howes, and A. Ivancich Structure-function relationships among heme peroxidases: new insights from electronic absorption, resonance Raman and multifrequence electron paramagnetic resonance spectroscopies K.M. Kadish, K.M. Smith, R. Guilard, Handbook of Porphyrin Science 2010 World Scientific Singapore 367 453
    • (2010) Handbook of Porphyrin Science , pp. 367-453
    • Smulevich, G.1    Feis, A.2    Howes, B.D.3    Ivancich, A.4
  • 42
    • 0030901963 scopus 로고    scopus 로고
    • Control of spin state by ring conformation of Iron (III) porphyrins. A novel model for the quantum-mixed intermediate spin state of ferric cytochrome c′ from photosynthetic bacteria
    • R.J. Cheng, P.Y. Chen, P.R. Gau, C.C. Chen, and S.M. Peng Control of spin state by ring conformation of Iron (III) porphyrins. A novel model for the quantum-mixed intermediate spin state of ferric cytochrome c′ from photosynthetic bacteria J. Am. Chem. Soc. 119 1997 2563 2569
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 2563-2569
    • Cheng, R.J.1    Chen, P.Y.2    Gau, P.R.3    Chen, C.C.4    Peng, S.M.5
  • 44
    • 0345515979 scopus 로고    scopus 로고
    • Alternative modes of substrate distortion in enzyme and antibody catalyzed ferrochelation reactions
    • DOI 10.1021/bi972616f
    • M.E. Blackwood Jr., T.S. Rush III, F. Romesberg, P.G. Schultz, and T.G. Spiro Alternative modes of substrate distortion in enzyme and antibody catalyzed ferrochelation reactions Biochemistry 37 1998 779 782 (Pubitemid 28060457)
    • (1998) Biochemistry , vol.37 , Issue.3 , pp. 779-782
    • Blackwood Jr., M.E.1    Rush III, T.S.2    Romesberg, F.3    Schultz, P.G.4    Spiro, T.G.5
  • 45
    • 0001386272 scopus 로고
    • Out-of-plane deformation modes in the resonance Raman spectra of metalloporphyrins and heme proteins
    • S. Choi, and T.G. Spiro Out-of-plane deformation modes in the resonance Raman spectra of metalloporphyrins and heme proteins J. Am. Chem. Soc. 105 1983 3683 3692
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 3683-3692
    • Choi, S.1    Spiro, T.G.2
  • 46
    • 0019887886 scopus 로고
    • Structural implication of the heme-linked ionization of horseradish peroxidase probed by the Fe-histidine stretching Raman line
    • J. Teraoka, and T. Kitagawa Structural implication of the heme-linked ionization of horseradish peroxidase probed by the Fe-histidine stretching Raman line J. Biol. Chem. 256 1981 3969 3977
    • (1981) J. Biol. Chem. , vol.256 , pp. 3969-3977
    • Teraoka, J.1    Kitagawa, T.2
  • 47
    • 0023692657 scopus 로고
    • Heme pocket interactions in cytochrome c peroxidase studied by site-directed mutagenesis and resonance Raman spectroscopy
    • G. Smulevich, J.M. Mauro, L.A. Fishel, A.M. English, J. Kraut, and T.G. Spiro Heme pocket interactions in cytochrome c peroxidase studied by site-directed mutagenesis and resonance Raman spectroscopy Biochemistry 27 1988 5477 5485
    • (1988) Biochemistry , vol.27 , pp. 5477-5485
    • Smulevich, G.1    Mauro, J.M.2    Fishel, L.A.3    English, A.M.4    Kraut, J.5    Spiro, T.G.6
  • 48
    • 0032474457 scopus 로고    scopus 로고
    • Spectroscopic characterization of recombinant pea cytosolic ascorbate peroxidase: Similarities and differences with cytochrome c peroxidase
    • DOI 10.1021/bi980111z
    • M. Nissum, F. Neri, D. Mandelman, T.L. Poulos, and G. Smulevich Spectroscopic characterization of recombinant pea cytosolic ascorbate peroxidase: similarities and differences with cytochrome c peroxidase Biochemistry 37 1998 8080 8087 (Pubitemid 28307069)
    • (1998) Biochemistry , vol.37 , Issue.22 , pp. 8080-8087
    • Nissum, M.1    Neri, F.2    Mandelman, D.3    Poulos, T.L.4    Smulevich, G.5
  • 49
    • 56749109668 scopus 로고    scopus 로고
    • Impact of distal side water and residue 315 on ligand binding to ferric Mycobacterium tuberculosis catalase-peroxidase (KatG)
    • K. Ranguelova, J. Suarez, L. Metlitsky, S. Yu, S.Z. Brejt, S.Z. Brejt, L. Zhao, J.P. Schelvis, and R.S. Magliozzo Impact of distal side water and residue 315 on ligand binding to ferric Mycobacterium tuberculosis catalase-peroxidase (KatG) Biochemistry 47 2008 12583 12592
    • (2008) Biochemistry , vol.47 , pp. 12583-12592
    • Ranguelova, K.1    Suarez, J.2    Metlitsky, L.3    Yu, S.4    Brejt, S.Z.5    Brejt, S.Z.6    Zhao, L.7    Schelvis, J.P.8    Magliozzo, R.S.9
  • 50
    • 0028589069 scopus 로고
    • Resonance Raman study of the active site of Coprinus cinereus peroxidase
    • G. Smulevich, A. Feis, C. Focardi, J. Tams, and K.G. Welinder Resonance Raman study of the active site of Coprinus cinereus peroxidase Biochemistry 33 1994 15425 15432
    • (1994) Biochemistry , vol.33 , pp. 15425-15432
    • Smulevich, G.1    Feis, A.2    Focardi, C.3    Tams, J.4    Welinder, K.G.5
  • 51
    • 0000355605 scopus 로고
    • Resonance Raman spectra of extracellular ligninase: Evidence for a heme active site similar to those of peroxidases
    • D. Kuila, M. Tien, J.A. Fee, and M.R. Ondrias Resonance Raman spectra of extracellular ligninase: evidence for a heme active site similar to those of peroxidases Biochemistry 24 1985 3394 3397
    • (1985) Biochemistry , vol.24 , pp. 3394-3397
    • Kuila, D.1    Tien, M.2    Fee, J.A.3    Ondrias, M.R.4
  • 52
    • 0024296692 scopus 로고
    • Spectral characterization of manganese peroxidase, an extracellular heme enzyme from the lignin-degrading basidiomycete, Phanerochaete chrysosporium
    • Y. Mino, H. Wariishi, N.J. Blackburn, T.M. Loehr, and M.H. Gold Spectral characterization of manganese peroxidase, an extracellular heme enzyme from the lignin-degrading basidiomycete, Phanerochaete chrysosporium J. Biol. Chem. 263 1988 7029 7036
    • (1988) J. Biol. Chem. , vol.263 , pp. 7029-7036
    • Mino, Y.1    Wariishi, H.2    Blackburn, N.J.3    Loehr, T.M.4    Gold, M.H.5
  • 54
    • 0032238226 scopus 로고    scopus 로고
    • Characterization of soybean seed coat peroxidase: Resonance Raman evidence for a structure-based classification of plant peroxidases
    • M. Nissum, A. Feis, and G. Smulevich Characterization of soybean seed coat peroxidase: resonance Raman evidence for a structure based classification of plant peroxidases Biospectroscopy 4 1998 355 364 (Pubitemid 128756557)
    • (1998) Biospectroscopy , vol.4 , Issue.6 , pp. 355-364
    • Nissum, M.1    Feis, A.2    Smulevich, G.3
  • 57
    • 0034687157 scopus 로고    scopus 로고
    • Redox potential measurements of the Mycobacterium tuberculosis heme protein KatG and the isoniazid-resistant enzyme KatG(S315T): Insights into isoniazid activation
    • N.L. Wengenack, H. Lopes, M.J. Kennedy, P. Tavares, A.S. Pereira, I. Moura, J.J.G. Moura, and F. Rusnak Redox potential measurements of the Mycobacterium tuberculosis heme protein KatG and the isoniazid-resistant enzyme KatG(S315T): insights into isoniazid activation Biochemistry 39 2000 11508 11513
    • (2000) Biochemistry , vol.39 , pp. 11508-11513
    • Wengenack, N.L.1    Lopes, H.2    Kennedy, M.J.3    Tavares, P.4    Pereira, A.S.5    Moura, I.6    Moura, J.J.G.7    Rusnak, F.8
  • 59
    • 41549088458 scopus 로고    scopus 로고
    • Elicitor and calatalse activity of conidia suspensions of various strains of Magnaporthe grisea in suspension-cultured cells of rice
    • DOI 10.1271/bbb.70684
    • S. Tanabe, N. Hayashi, Y. Nishizawa, H. Yamane, N. Shibuya, and E. Minami Elicitor and catalase activity of conidia suspensions of various strains of Magnaporthe grisea in suspension-cultured cells of rice Biosci. Biotechnol. Biochem. 72 2008 889 892 (Pubitemid 351463678)
    • (2008) Bioscience, Biotechnology and Biochemistry , vol.72 , Issue.3 , pp. 889-892
    • Tanabe, S.1    Hayashi, N.2    Nishizawa, Y.3    Yamane, H.4    Shibuya, N.5    Minami, E.6
  • 60
    • 0000121196 scopus 로고
    • Purification and characterization of pea cytosolic ascorbate peroxidase
    • R. Mittler, and B.A. Zilinskas Purification and characterization of pea cytosolic ascorbate peroxidase Plant Physiol. 97 1991 962 968 (Pubitemid 21914315)
    • (1991) Plant Physiology , vol.97 , Issue.3 , pp. 962-968
    • Mittler, R.1    Zilinskas, B.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.