메뉴 건너뛰기




Volumn 279, Issue 2, 2012, Pages 348-357

Identification of Tyr74 and Tyr177 as substrate oxidation sites in cationic cell wall-bound peroxidase from Populus alba L.

Author keywords

electron transfer; lignification; plant peroxidase; Populus alba L.; protein engineering

Indexed keywords

CATIONIC CELL WALL BOUND PEROXIDASE; GUAIACOL; PEROXIDASE; PHENYLALANINE; REAGENT; RECOMBINANT PROTEIN; SYRINGALDAZINE; SYRINGOL; TYROSINE; UNCLASSIFIED DRUG;

EID: 84855438243     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2011.08429.x     Document Type: Article
Times cited : (19)

References (53)
  • 1
    • 0035832912 scopus 로고    scopus 로고
    • Oxidation of cinnamyl alcohols and aldehydes by a basic peroxidase from lignifying Zinnia elegans hypocotyls
    • DOI 10.1016/S0031-9422(01)00050-4, PII S0031942201000504
    • Barcelõ AR, &, Pomar F, (2001) Oxidation of cinnamyl alcohols and aldehydes by a basic peroxidase from lignifying Zinnia elegans hypocotyls. Phytochemistry 57, 1105-1113. (Pubitemid 32625586)
    • (2001) Phytochemistry , vol.57 , Issue.7 , pp. 1105-1113
    • Barcelo A.Ros1    Pomar, F.2
  • 2
    • 0042823502 scopus 로고    scopus 로고
    • A lignin-specific peroxidase in tobacco whose antisense suppression leads to vascular tissue modification
    • DOI 10.1016/S0031-9422(03)00212-7
    • Blee KA, Choi JW, O'Connell AP, Schuch W, Lewis NG, &, Bolwell GP, (2003) A lignin-specific peroxidase in tobacco whose antisense suppression leads to vascular tissue modification. Phytochemistry 64, 163-176. (Pubitemid 37101802)
    • (2003) Phytochemistry , vol.64 , Issue.1 , pp. 163-176
    • Bleea, K.A.1    Choib, J.W.2    O'Connella, A.P.3    Schuchc, W.4    Lewis, N.G.5    Bolwell, G.P.6
  • 4
    • 0035909072 scopus 로고    scopus 로고
    • Differential activity and structure of highly similar peroxidases. Spectroscopic, crystallographic, and enzymatic analyses of lignifying Arabidopsis thaliana peroxidase A2 and horseradish peroxidase A2
    • DOI 10.1021/bi010661o
    • Nielsen KL, Indiani C, Henriksen A, Feis A, Becucci M, Gajhede M, Smulevich G, &, Welinder KG, (2001) Differential activity and structure of highly similar peroxidases. Spectroscopic, crystallographic, and enzymatic analyses of lignifying Arabidopsis thaliana peroxidase A2 and horseradish peroxidase A2. Biochemistry 40, 11013-11021. (Pubitemid 32847967)
    • (2001) Biochemistry , vol.40 , Issue.37 , pp. 11013-11021
    • Nielsen, K.L.1    Indiani, C.2    Henriksen, A.3    Feis, A.4    Becucci, M.5    Gajhede, M.6    Smulevich, G.7    Welinder, K.G.8
  • 6
    • 37549046767 scopus 로고    scopus 로고
    • Role of Tyr residues on the protein surface of cationic cell-wall-peroxidase (CWPO-C) from poplar: Potential oxidation sites for oxidative polymerization of lignin
    • Sasaki S, Nonaka D, Wariishi H, Tsutsumi Y, &, Kondo R, (2008) Role of Tyr residues on the protein surface of cationic cell-wall-peroxidase (CWPO-C) from poplar: potential oxidation sites for oxidative polymerization of lignin. Phytochemistry 69, 348-355.
    • (2008) Phytochemistry , vol.69 , pp. 348-355
    • Sasaki, S.1    Nonaka, D.2    Wariishi, H.3    Tsutsumi, Y.4    Kondo, R.5
  • 7
    • 0007705692 scopus 로고
    • Lignin biosynthesis in woody angiosperm tissue. III. Isolation of substrate-specific peroxidase related to the dehydrogenative polymerization of sinapyl and coniferyl alcohols from Populus callus cultures
    • Tsutsumi Y, Nishida T, &, Sakai K, (1994) Lignin biosynthesis in woody angiosperm tissue. III. Isolation of substrate-specific peroxidase related to the dehydrogenative polymerization of sinapyl and coniferyl alcohols from Populus callus cultures. Mokuzai Gakkaishi 40, 1348-1354.
    • (1994) Mokuzai Gakkaishi , vol.40 , pp. 1348-1354
    • Tsutsumi, Y.1    Nishida, T.2    Sakai, K.3
  • 8
    • 0031645821 scopus 로고    scopus 로고
    • Substrate-specific peroxidases in woody angiosperms and gymnosperms participate in regulating the dehydrogenative polymerization of syringyl and guaiacyl type lignins
    • Tsutsumi Y, Matsui K, &, Sakai K, (1998) Substrate-specific peroxidases in woody angiosperms and gymnosperm participate in regulating the dehydrogenative polymerization of syringyl and guaiacyl type lignins. Holzforschung 52, 275-281. (Pubitemid 128620913)
    • (1998) Holzforschung , vol.52 , Issue.3 , pp. 275-281
    • Tsutsumi, Y.1    Matsui, K.2    Sakai, K.3
  • 9
    • 0041936701 scopus 로고    scopus 로고
    • Sinapyl alcohol-specific peroxidase isoenzyme catalyzes the formation of the dehydrogenative polymer from sinapyl alcohol
    • Aoyama W, Sasaki S, Matsumura S, Hirai H, Tsutsumi Y, &, Nishida T, (2002) Sinapyl alcohol-specific peroxidase isoenzyme catalyzes the formation of the dehydrogenative polymer from sinapyl alcohol. J Wood Sci 48, 497-504. (Pubitemid 37292758)
    • (2002) Journal of Wood Science , vol.48 , Issue.6 , pp. 497-504
    • Aoyama, W.1    Sasaki, S.2    Matsumura, S.3    Mitsunaga, T.4    Hirai, H.5    Tsutsumi, Y.6    Nishida, T.7
  • 10
    • 1642377866 scopus 로고    scopus 로고
    • Lignin dehydrogenative polymerization mechanism: A poplar cell wall peroxidase directly oxidizes polymer lignin and produces in vitro dehydrogenative polymer rich in β-O-4 linkage
    • DOI 10.1016/S0014-5793(04)00224-8, PII S0014579304002248
    • Sasaki S, Nishida T, Tsutsumi Y, &, Kondo R, (2004) Lignin dehydrogenative polymerization mechanism: a poplar cell wall peroxidase directly oxidizes polymer lignin and produces in vitro dehydrogenative polymer rich in β-O-4 linkage. FEBS Lett 562, 197-201. (Pubitemid 38388471)
    • (2004) FEBS Letters , vol.562 , Issue.1-3 , pp. 197-201
    • Sasaki, S.1    Nishida, T.2    Tsutsumi, Y.3    Kondo, R.4
  • 11
    • 0032023777 scopus 로고    scopus 로고
    • Protein radicals in enzyme catalysis
    • Stubbe J, &, van der Donk W, (1998) Protein radicals in enzyme catalysis. Chem Rev 98, 705-762. (Pubitemid 128631440)
    • (1998) Chemical Reviews , vol.98 , Issue.2 , pp. 705-762
    • Stubbe, J.1    Van Der Donk, W.A.2
  • 12
    • 38949176067 scopus 로고    scopus 로고
    • Site-directed mutagenesis of the catalytic tryptophan environment in Pleurotus eryngii versatile peroxidase
    • DOI 10.1021/bi7020298
    • Ruiz-Duenas FJ, Morales M, Mate MJ, Romero A, Martinez MJ, Smith AT, &, Martinez AT, (2008) Site-directed mutagenesis of the catalytic tryptophan environment in Pleurotus eryngii versatile peroxidase. Biochemistry 47, 1685-1695. (Pubitemid 351231218)
    • (2008) Biochemistry , vol.47 , Issue.6 , pp. 1685-1695
    • Ruiz-Duenas, F.J.1    Morales, M.2    Mate, M.J.3    Romero, A.4    Martinez, M.J.5    Smith, A.T.6    Martinez, A.T.7
  • 13
    • 65549133817 scopus 로고    scopus 로고
    • Protein radicals in fungal versatile peroxidase: Catalytic tryptophan radical in both compound i and compound II and studies on W164Y, W164H, and W164S variants
    • Ruiz-Duenas FJ, Pogni R, Morales M, Giansanti S, Mate MJ, Romero A, Martinez MJ, Basosi R, &, Martinez AT, (2009) 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.
    • (2009) J Biol Chem , vol.284 , pp. 7986-7994
    • Ruiz-Duenas, F.J.1    Pogni, R.2    Morales, M.3    Giansanti, S.4    Mate, M.J.5    Romero, A.6    Martinez, M.J.7    Basosi, R.8    Martinez, A.T.9
  • 14
    • 0032573035 scopus 로고    scopus 로고
    • Two substrate interaction sites in lignin peroxidase revealed by site- directed mutagenesis
    • DOI 10.1021/bi981633h
    • Doyle WA, Blodig W, Veitch NC, Piontek K, &, Smith AT, (1998) Two substrate interaction sites in lignin peroxidase revealed by site-directed mutagenesis. Biochemistry 37, 15097-15105. (Pubitemid 28503237)
    • (1998) Biochemistry , vol.37 , Issue.43 , pp. 15097-15105
    • Doyle, W.A.1    Blodig, W.2    Veitch, N.C.3    Piontek, K.4    Smith, A.T.5
  • 16
    • 0017900576 scopus 로고
    • Functional modifications of aspartate transcarbamylase induced by nitration with tetranitromethane
    • Landfear SM, Lipscomb WN, &, Evans DR, (1978) Functional modifications of aspartate transcarbamylase induced by nitration with tetranitromethane. J Biol Chem 253, 3988-3996. (Pubitemid 8361610)
    • (1978) Journal of Biological Chemistry , vol.253 , Issue.11 , pp. 3988-3996
    • Landfear, S.M.1    Lipscomb, W.N.2    Evans, D.R.3
  • 17
    • 79958767629 scopus 로고    scopus 로고
    • Determination of a catalytic tyrosine in Trametes cervina lignin peroxidase with chemical modification techniques
    • Miki Y, Ichinose H, &, Wariishi H, (2011) Determination of a catalytic tyrosine in Trametes cervina lignin peroxidase with chemical modification techniques. Biotechnol Lett 33, 1423-1427.
    • (2011) Biotechnol Lett , vol.33 , pp. 1423-1427
    • Miki, Y.1    Ichinose, H.2    Wariishi, H.3
  • 18
    • 79958024318 scopus 로고    scopus 로고
    • Probing structural differences between PrP (C) and PrP (Sc) by surface nitration and acetylation: Evidence of conformational change in the C-terminus
    • Gong B, Ramos A, Vazquez-Fernandez E, Silva CJ, Alonso J, Liu Z, &, Requena JR, (2011) Probing structural differences between PrP (C) and PrP (Sc) by surface nitration and acetylation: evidence of conformational change in the C-terminus. Biochemistry 50, 4963-4972.
    • (2011) Biochemistry , vol.50 , pp. 4963-4972
    • Gong, B.1    Ramos, A.2    Vazquez-Fernandez, E.3    Silva, C.J.4    Alonso, J.5    Liu, Z.6    Requena, J.R.7
  • 19
    • 0014619592 scopus 로고
    • Reaction of tetranitromethane with sulfhydryl groups in proteins
    • Sokolovsky M, Harell D, &, Riordan JF, (1969) Reaction of tetranitromethane with sulfhydryl groups in proteins. Biochemistry 8, 4740-4745.
    • (1969) Biochemistry , vol.8 , pp. 4740-4745
    • Sokolovsky, M.1    Harell, D.2    Riordan, J.F.3
  • 20
    • 0035798657 scopus 로고    scopus 로고
    • The critical role of the proximal calcium ion in the structural properties of horseradish peroxidase
    • Howes BD, Feis A, Raimondi L, Indiani C, &, Smulevich G, (2001) The critical role of the proximal calcium ion in the structural properties of horseradish peroxidase. J Biol Chem 276, 40704-40711.
    • (2001) J Biol Chem , vol.276 , pp. 40704-40711
    • Howes, B.D.1    Feis, A.2    Raimondi, L.3    Indiani, C.4    Smulevich, G.5
  • 21
    • 33750898437 scopus 로고    scopus 로고
    • The cationic cell-wall-peroxidase having oxidation ability for polymeric substrate participates in the late stage of lignification of Populus alba L
    • DOI 10.1007/s11103-006-9057-3
    • Sasaki S, Baba K, Nishida T, Tsutsumi Y, &, Kondo R, (2006) The cationic cell-wall-peroxidase having oxidation ability for polymeric substrate participates in the late stage of lignification of Populus alba L. Plant Mol Biol 62, 797-807. (Pubitemid 44730319)
    • (2006) Plant Molecular Biology , vol.62 , Issue.6 , pp. 797-807
    • Sasaki, S.1    Baba, K.2    Nishida, T.3    Tsutsumi, Y.4    Kondo, R.5
  • 23
    • 0030587532 scopus 로고    scopus 로고
    • Heterologous expression and reconstitution of fungal Mn peroxidase
    • DOI 10.1006/abbi.1996.0413
    • Whitwam R, &, Tien M, (1996) Heterologous expression and reconstitution of fungal Mn peroxidase. Arch Biochem Biophys 333, 439-446. (Pubitemid 26304912)
    • (1996) Archives of Biochemistry and Biophysics , vol.333 , Issue.2 , pp. 439-446
    • Whitwam, R.1    Tien, M.2
  • 25
    • 70349466798 scopus 로고    scopus 로고
    • Escherichia coli expression and in vitro activation of a unique ligninolytic peroxidase that has a catalytic tyrosine residue
    • Miki Y, Morales M, Ruiz-Duenas FJ, Martinez MJ, Wariishi H, &, Martinez AT, (2009) Escherichia coli expression and in vitro activation of a unique ligninolytic peroxidase that has a catalytic tyrosine residue. Protein Expr Purif 68, 208-214.
    • (2009) Protein Expr Purif , vol.68 , pp. 208-214
    • Miki, Y.1    Morales, M.2    Ruiz-Duenas, F.J.3    Martinez, M.J.4    Wariishi, H.5    Martinez, A.T.6
  • 26
    • 0031648468 scopus 로고    scopus 로고
    • A new derivatizing agent, trimethylammoniopropyl methanethiosulphonate, is efficient for preparation of recombinant brain-derived neurotrophic factor from inclusion bodies
    • Inoue M, Akimaru J, Nishikawa T, Seki N, &, Yamada H, (1998) A new derivatizing agent, trimethylammoniopropyl methanethiosulphonate, is efficient for preparation of recombinant brain-derived neurotrophic factor from inclusion bodies. Biotechnol Appl Biochem 28 (Pt 3), 207-213. (Pubitemid 28564413)
    • (1998) Biotechnology and Applied Biochemistry , vol.28 , Issue.3 , pp. 207-213
    • Inoue, M.1    Akimaru, J.2    Nishikawa, T.3    Seki, N.4    Yamada, H.5
  • 29
    • 0035951308 scopus 로고    scopus 로고
    • Crystal structures of pristine and oxidatively processed lignin peroxidase expressed in Escherichia coli and of the W171F variant that eliminates the redox active tryptophan 171. Implications for the reaction mechanism
    • DOI 10.1006/jmbi.2000.4346
    • Blodig W, Smith AT, Doyle WA, &, Piontek K, (2001) Crystal structures of pristine and oxidatively processed lignin peroxidase expressed in Escherichia coli and of the W171F variant that eliminates the redox active tryptophan 171. Implications for the reaction mechanism. J Mol Biol 305, 851-861. (Pubitemid 33030031)
    • (2001) Journal of Molecular Biology , vol.305 , Issue.4 , pp. 851-861
    • Blodig, W.1    Smith, A.T.2    Doyle, W.A.3    Piontek, K.4
  • 30
    • 70349522119 scopus 로고    scopus 로고
    • Spectroscopic evidence for an engineered, catalytically active Trp radical that creates the unique reactivity of lignin peroxidase
    • Smith AT, Doyle WA, Dorlet P, &, Ivancich A, (2009) Spectroscopic evidence for an engineered, catalytically active Trp radical that creates the unique reactivity of lignin peroxidase. Proc Natl Acad Sci USA 106, 16084-16089.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 16084-16089
    • Smith, A.T.1    Doyle, W.A.2    Dorlet, P.3    Ivancich, A.4
  • 31
    • 0027056273 scopus 로고
    • Crystal structure of a complex between electron transfer partners, cytochrome c peroxidase and cytochrome c
    • Pelletier H, &, Kraut J, (1992) Crystal structure of a complex between electron transfer partners, cytochrome c peroxidase and cytochrome c. Science 258, 1748-1755. (Pubitemid 23087339)
    • (1992) Science , vol.258 , Issue.5089 , pp. 1748-1755
    • Pelletier, H.1    Kraut, J.2
  • 32
    • 0343618384 scopus 로고    scopus 로고
    • Reaction of bovine cytochrome c oxidase with hydrogen peroxide produces a tryptophan cation radical and a porphyrin cation radical
    • DOI 10.1021/bi992614q
    • Rigby SE, Junemann S, Rich PR, &, Heathcote P, (2000) Reaction of bovine cytochrome c oxidase with hydrogen peroxide produces a tryptophan cation radical and a porphyrin cation radical. Biochemistry 39, 5921-5928. (Pubitemid 30327065)
    • (2000) Biochemistry , vol.39 , Issue.20 , pp. 5921-5928
    • Rigby, S.E.J.1    Junemann, S.2    Rich, P.R.3    Heathcote, P.4
  • 33
    • 0035849509 scopus 로고    scopus 로고
    • Comparative electron paramagnetic resonance study of radical intermediates in turnip peroxidase isozymes
    • DOI 10.1021/bi002826j
    • Ivancich A, Mazza G, &, Desbois A, (2001) Comparative electron paramagnetic resonance study of radical intermediates in turnip peroxidase isozymes. Biochemistry 40, 6860-6866. (Pubitemid 32538232)
    • (2001) Biochemistry , vol.40 , Issue.23 , pp. 6860-6866
    • Ivancich, A.1    Mazza, G.2    Desbois, A.3
  • 34
    • 3042773983 scopus 로고    scopus 로고
    • A new method of identifying the site of tyrosyl radicals in proteins
    • DOI 10.1529/biophysj.104.041046
    • Svistunenko DA, &, Cooper CE, (2004) A new method of identifying the site of tyrosyl radicals in proteins. Biophys J 87, 582-595. (Pubitemid 38880111)
    • (2004) Biophysical Journal , vol.87 , Issue.1 , pp. 582-595
    • Svistunenko, D.A.1    Cooper, C.E.2
  • 37
    • 1042265206 scopus 로고    scopus 로고
    • Identification of Tyr504 as an Alternative Tyrosyl Radical Site in Human Prostaglandin H Synthase-2
    • DOI 10.1021/bi035717o
    • Rogge CE, Liu W, Wu G, Wang LH, Kulmacz RJ, &, Tsai AL, (2004) Identification of Tyr504 as an alternative tyrosyl radical site in human prostaglandin H synthase-2. Biochemistry 43, 1560-1568. (Pubitemid 38200561)
    • (2004) Biochemistry , vol.43 , Issue.6 , pp. 1560-1568
    • Rogge, C.E.1    Liu, W.2    Wu, G.3    Wang, L.-H.4    Kulmacz, R.J.5    Tsai, A.-L.6
  • 38
    • 1542379915 scopus 로고    scopus 로고
    • Evidence for Radical Formation at Tyr-353 in Mycobacterium tuberculosis Catalase-Peroxidase (KatG)
    • DOI 10.1074/jbc.M311884200
    • Zhao X, Girotto S, Yu S, &, Magliozzo RS, (2004) Evidence for radical formation at Tyr-353 in Mycobacterium tuberculosis catalase-peroxidase (KatG). J Biol Chem 279, 7606-7612. (Pubitemid 38294640)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.9 , pp. 7606-7612
    • Zhao, X.1    Girotto, S.2    Yu, S.3    Magliozzo, R.S.4
  • 39
    • 0242414727 scopus 로고    scopus 로고
    • Protein-Based Radicals in the Catalase-Peroxidase of Synechocystis PCC6803: A Multifrequency EPR Investigation of Wild-Type and Variants on the Environment of the Heme Active Site
    • DOI 10.1021/ja035582+
    • Ivancich A, Jakopitsch C, Auer M, Un S, &, Obinger C, (2003) Protein-based radicals in the catalase-peroxidase of Synechocystis PCC6803: a multifrequency EPR investigation of wild-type and variants on the environment of the heme active site. J Am Chem Soc 125, 14093-14102. (Pubitemid 37420914)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.46 , pp. 14093-14102
    • Ivancich, A.1    Jakopitsch, C.2    Auer, M.3    Un, S.4    Obinger, C.5
  • 41
    • 0037123359 scopus 로고    scopus 로고
    • Analysis and expression of the class III peroxidase large gene family in Arabidopsis thaliana
    • DOI 10.1016/S0378-1119(02)00465-1, PII S0378111902004651
    • Tognolli M, Penel C, Greppin H, &, Simon P, (2002) Analysis and expression of the class III peroxidase large gene family in Arabidopsis thaliana. Gene 288, 129-138. (Pubitemid 34595370)
    • (2002) Gene , vol.288 , Issue.1-2 , pp. 129-138
    • Tognolli, M.1    Penel, C.2    Greppin, H.3    Simon, P.4
  • 43
    • 33644835373 scopus 로고    scopus 로고
    • Cloning and molecular characterization of the basic peroxidase isoenzyme from Zinnia elegans, an enzyme involved in lignin biosynthesis
    • DOI 10.1104/pp.105.069674
    • Gabaldon C, Lopez-Serrano M, Pedreno MA, &, Barcelõ AR, (2005) Cloning and molecular characterization of the basic peroxidase isoenzyme from Zinnia elegans, an enzyme involved in lignin biosynthesis. Plant Physiol 139, 1138-1154. (Pubitemid 43786818)
    • (2005) Plant Physiology , vol.139 , Issue.3 , pp. 1138-1154
    • Gabaldon, C.1    Lopez-Serrano, M.2    Pedreno, M.A.3    Barcelo, A.R.4
  • 44
    • 33646494182 scopus 로고    scopus 로고
    • Monolignol oxidation by xylem peroxidase isoforms of Norway spruce (Picea abies) and silver birch (Betula pendula)
    • Marjamaa K, Kukkola E, Lundell T, Karhunen P, Saranpaa P, &, Fagerstedt KV, (2006) Monolignol oxidation by xylem peroxidase isoforms of Norway spruce (Picea abies) and silver birch (Betula pendula). Tree Physiol 26, 605-611.
    • (2006) Tree Physiol , vol.26 , pp. 605-611
    • Marjamaa, K.1    Kukkola, E.2    Lundell, T.3    Karhunen, P.4    Saranpaa, P.5    Fagerstedt, K.V.6
  • 45
    • 0033605084 scopus 로고    scopus 로고
    • The crystal structure of lignin peroxidase at 1.70 A resolution reveals a hydroxy group on the C(β) of tryptophan 171: A novel radical site formed during the redox cycle
    • DOI 10.1006/jmbi.1998.2507
    • Choinowski T, Blodig W, Winterhalter KH, &, Piontek K, (1999) The crystal structure of lignin peroxidase at 1.70 A resolution reveals a hydroxy group on the cbeta of tryptophan 171: a novel radical site formed during the redox cycle. J Mol Biol 286, 809-827. (Pubitemid 29106220)
    • (1999) Journal of Molecular Biology , vol.286 , Issue.3 , pp. 809-827
    • Choinowski, T.1    Blodig, W.2    Winterhalter, K.H.3    Piontek, K.4
  • 46
    • 0030848480 scopus 로고    scopus 로고
    • Introduction of novel substrate oxidation into cytochrome c peroxidase by cavity complementation: Oxidation of 2-aminothiazole and covalent modification of the enzyme
    • DOI 10.1021/bi9708038
    • Musah RA, &, Goodin DB, (1997) Introduction of novel substrate oxidation into cytochrome c peroxidase by cavity complementation: oxidation of 2-aminothiazole and covalent modification of the enzyme. Biochemistry 36, 11665-11674. (Pubitemid 27424091)
    • (1997) Biochemistry , vol.36 , Issue.39 , pp. 11665-11674
    • Musah, R.A.1    Goodin, D.B.2
  • 47
    • 0037137215 scopus 로고    scopus 로고
    • Radical formation at Tyr39 and Tyr153 following reaction of yeast cytochrome c peroxidase with hydrogen peroxide
    • DOI 10.1021/bi026122g
    • Zhang H, He S, &, Mauk AG, (2002) Radical formation at Tyr39 and Tyr153 following reaction of yeast cytochrome c peroxidase with hydrogen peroxide. Biochemistry 41, 13507-13513. (Pubitemid 35332686)
    • (2002) Biochemistry , vol.41 , Issue.46 , pp. 13507-13513
    • Zhang, H.1    He, S.2    Mauk, A.G.3
  • 49
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL workspace: A web-based environment for protein structure homology modelling
    • DOI 10.1093/bioinformatics/bti770
    • Arnold K, Bordoli L, Kopp J, &, Schwede T, (2006) The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling. Bioinformatics 22, 195-201. (Pubitemid 43205406)
    • (2006) Bioinformatics , vol.22 , Issue.2 , pp. 195-201
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 51
    • 77049140918 scopus 로고
    • Intermediate compound formation with peroxidase and strong oxidizing agents
    • George P, (1953) Intermediate compound formation with peroxidase and strong oxidizing agents. J Biol Chem 201, 413-426.
    • (1953) J Biol Chem , vol.201 , pp. 413-426
    • George, P.1
  • 52
    • 0000736222 scopus 로고
    • Use of syringaldazine in a photometric method for estimating 'free' chlorine in water
    • Bauer R, &, Rupe CO, (1971) Use of syringaldazine in a photometric method for estimating 'free' chlorine in water. Anal Chem 43, 421-425.
    • (1971) Anal Chem , vol.43 , pp. 421-425
    • Bauer, R.1    Rupe, C.O.2
  • 53
    • 0027096634 scopus 로고
    • Manganese(II) oxidation by manganese peroxidase from the basidiomycete Phanerochaete chrysosporium. Kinetic mechanism and role of chelators
    • 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. (Pubitemid 23088173)
    • (1992) Journal of Biological Chemistry , vol.267 , Issue.33 , pp. 23688-23695
    • Wariishi, H.1    Valli, K.2    Gold, M.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.