메뉴 건너뛰기




Volumn 466, Issue , 2015, Pages 253-262

Catalytic surface radical in dye-decolorizing peroxidase: A computational, spectroscopic and site-directed mutagenesis study

Author keywords

Catalytic protein radical; Dye decolorizing peroxidase; EPR spectroscopy; Molecular docking; QM MM; Site directed mutagenesis

Indexed keywords

ARGININE; CYSTEINE; DYE DECOLORIZING PEROXIDASE; PEROXIDASE; RADICAL; RECOMBINANT ENZYME; TRYPTOPHAN; TYROSINE; UNCLASSIFIED DRUG; COLORING AGENT; FREE RADICAL; FUNGAL PROTEIN; HEMOPROTEIN; MUTANT PROTEIN; RECOMBINANT PROTEIN;

EID: 84923238755     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20141211     Document Type: Article
Times cited : (86)

References (55)
  • 1
    • 67349235552 scopus 로고    scopus 로고
    • DyP-type peroxidases comprise a novel heme peroxidase family
    • CrossRef PubMed
    • Sugano, Y. (2009) DyP-type peroxidases comprise a novel heme peroxidase family. Cell. Mol. Life Sci. 66, 1387-1403 CrossRef PubMed
    • (2009) Cell. Mol. Life Sci. , vol.66 , pp. 1387-1403
    • Sugano, Y.1
  • 3
    • 84895209619 scopus 로고    scopus 로고
    • Structural and functional features of peroxidases with a potential as industrial biocatalysts
    • Torres, E. and Ayala, M., eds Springer-Verlag, Berlin CrossRef
    • Ruiz-Dueñas, F.J. and Martínez, A.T. (2010) Structural and functional features of peroxidases with a potential as industrial biocatalysts. In Biocatalysts Based on Heme Peroxidases (Torres, E. and Ayala, M., eds), pp. 37-59, Springer-Verlag, Berlin CrossRef
    • (2010) Biocatalysts Based on Heme Peroxidases , pp. 37-59
    • Ruiz-Dueñas, F.J.1    Martínez, A.T.2
  • 4
    • 84891879043 scopus 로고    scopus 로고
    • DyP-type peroxidases: A promising and versatile class of enzymes
    • CrossRef PubMed
    • Colpa, D.I., Fraaije, M.W. and van Bloois, E. (2014) DyP-type peroxidases: a promising and versatile class of enzymes. J. Ind. Microbiol. Biotechnol. 41, 1-7 CrossRef PubMed
    • (2014) J. Ind. Microbiol. Biotechnol. , vol.41 , pp. 1-7
    • Colpa, D.I.1    Fraaije, M.W.2    Van Bloois, E.3
  • 5
    • 0345472013 scopus 로고    scopus 로고
    • Purification and characterization of a novel peroxidase from Geotrichum candidum Dec 1 involved in decolorization of dyes
    • PubMed
    • Kim, S.J. and Shoda, M. (1999) Purification and characterization of a novel peroxidase from Geotrichum candidum Dec 1 involved in decolorization of dyes. Appl. Environ. Microbiol. 65, 1029-1035 PubMed
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 1029-1035
    • Kim, S.J.1    Shoda, M.2
  • 7
    • 84870571391 scopus 로고    scopus 로고
    • Crystal structures of dye-decolorizing peroxidase with ascorbic acid and 2,6-dimethoxyphenol
    • CrossRef PubMed
    • Yoshida, T., Tsuge, H., Hisabori, T. and Sugano, Y. (2012) Crystal structures of dye-decolorizing peroxidase with ascorbic acid and 2,6-dimethoxyphenol. FEBS Lett. 586, 4351-4356 CrossRef PubMed
    • (2012) FEBS Lett. , vol.586 , pp. 4351-4356
    • Yoshida, T.1    Tsuge, H.2    Hisabori, T.3    Sugano, Y.4
  • 8
    • 84879419989 scopus 로고    scopus 로고
    • Substrate oxidation by dye-decolorizing peroxidases (DyPs) from wood- and litter-degrading agaricomycetes compared to other fungal and plant heme-peroxidases
    • CrossRef
    • Liers, C., Pecyna, M.J., Kellner, H., Worrich, A., Zorn, H., Steffen, K.T., Hofrichter, M. and Ullrich, R. (2013) Substrate oxidation by dye-decolorizing peroxidases (DyPs) from wood- and litter-degrading agaricomycetes compared to other fungal and plant heme-peroxidases. Appl. Microbiol. Biotechnol. 87, 5839-5849 CrossRef
    • (2013) Appl. Microbiol. Biotechnol. , vol.87 , pp. 5839-5849
    • Liers, C.1    Pecyna, M.J.2    Kellner, H.3    Worrich, A.4    Zorn, H.5    Steffen, K.T.6    Hofrichter, M.7    Ullrich, R.8
  • 9
    • 84873638013 scopus 로고    scopus 로고
    • First crystal structure of a fungal high-redox potential dye-decolorizing peroxidase: Substrate interaction sites and long-range electron transfer
    • CrossRef PubMed
    • Strittmatter, E., Liers, C., Ullrich, R., Wachter, S., Hofrichter, M., Plattner, D.A. and Piontek, K. (2013) First crystal structure of a fungal high-redox potential dye-decolorizing peroxidase: substrate interaction sites and long-range electron transfer. J. Biol. Chem. 288, 4095-4102 CrossRef PubMed
    • (2013) J. Biol. Chem. , vol.288 , pp. 4095-4102
    • Strittmatter, E.1    Liers, C.2    Ullrich, R.3    Wachter, S.4    Hofrichter, M.5    Plattner, D.A.6    Piontek, K.7
  • 12
    • 34548809711 scopus 로고    scopus 로고
    • Crystal structures of two novel dye-decolorizing peroxidases reveal a β-barrel fold with a conserved heme-binding motif
    • CrossRef PubMed
    • Zubieta, C., Krishna, S.S., Kapoor, M., Kozbial, P., McMullan, D., Axelrod, H.L., Miller, M.D., Abdubek, P., Ambing, E., Astakhova, T. et al. (2007) Crystal structures of two novel dye-decolorizing peroxidases reveal a β-barrel fold with a conserved heme-binding motif. Proteins 69, 223-233 CrossRef PubMed
    • (2007) Proteins , vol.69 , pp. 223-233
    • Zubieta, C.1    Krishna, S.S.2    Kapoor, M.3    Kozbial, P.4    McMullan, D.5    Axelrod, H.L.6    Miller, M.D.7    Abdubek, P.8    Ambing, E.9    Astakhova, T.10
  • 14
    • 79958818206 scopus 로고    scopus 로고
    • Characterization of dye-decolorizing peroxidases from Rhodococcus jostii RHA1
    • CrossRef PubMed
    • Roberts, J.N., Singh, R., Grigg, J.C., Murphy, M. E. P., Bugg, T. D. H. and Eltis, L.D. (2011) Characterization of dye-decolorizing peroxidases from Rhodococcus jostii RHA1. Biochemistry 50, 5108-5119 CrossRef PubMed
    • (2011) Biochemistry , vol.50 , pp. 5108-5119
    • Roberts, J.N.1    Singh, R.2    Grigg, J.C.3    Murphy, M.E.P.4    Bugg, T.D.H.5    Eltis, L.D.6
  • 15
    • 84871590888 scopus 로고    scopus 로고
    • Identification and characterization of a multifunctional dye peroxidase from a lignin-reactive bacterium
    • CrossRef PubMed
    • Brown, M.E., Barros, T. and Chang, M. C. Y. (2012) Identification and characterization of a multifunctional dye peroxidase from a lignin-reactive bacterium. ACS Chem. Biol. 7, 2074-2081 CrossRef PubMed
    • (2012) ACS Chem. Biol. , vol.7 , pp. 2074-2081
    • Brown, M.E.1    Barros, T.2    Chang, M.C.Y.3
  • 16
    • 0034127006 scopus 로고    scopus 로고
    • Efficient heterologous expression in Aspergillus oryzae of a unique dye decolorizing peroxidase, DyP, of Geotrichum candidum Dec 1
    • CrossRef PubMed
    • Sugano, Y., Nakano, R., Sasaki, K. and Shoda, M. (2000) Efficient heterologous expression in Aspergillus oryzae of a unique dye decolorizing peroxidase, DyP, of Geotrichum candidum Dec 1. Appl. Environ. Microbiol. 66, 1754-1758 CrossRef PubMed
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 1754-1758
    • Sugano, Y.1    Nakano, R.2    Sasaki, K.3    Shoda, M.4
  • 17
    • 4143083743 scopus 로고    scopus 로고
    • Role of H164 in a unique dye-decolorizing heme peroxidase DyP
    • CrossRef PubMed
    • Sugano, Y., Ishii, Y. and Shoda, M. (2004) Role of H164 in a unique dye-decolorizing heme peroxidase DyP. Biochem. Biophys. Res. Commun. 322, 126-132 CrossRef PubMed
    • (2004) Biochem. Biophys. Res. Commun. , vol.322 , pp. 126-132
    • Sugano, Y.1    Ishii, Y.2    Shoda, M.3
  • 18
    • 76849083614 scopus 로고    scopus 로고
    • DyP-like peroxidases of the jelly fungus Auricularia auricula-judae oxidize nonphenolic lignin model compounds and high-redox potential dyes
    • CrossRef PubMed
    • Liers, C., Bobeth, C., Pecyna, M., Ullrich, R. and Hofrichter, M. (2010) DyP-like peroxidases of the jelly fungus Auricularia auricula-judae oxidize nonphenolic lignin model compounds and high-redox potential dyes. Appl. Microbiol. Biotechnol. 85, 1869-1879 CrossRef PubMed
    • (2010) Appl. Microbiol. Biotechnol. , vol.85 , pp. 1869-1879
    • Liers, C.1    Bobeth, C.2    Pecyna, M.3    Ullrich, R.4    Hofrichter, M.5
  • 19
    • 84908120137 scopus 로고    scopus 로고
    • Heterologous expression and physicochemical characterization of a fungal dye-decolorizing peroxidase from Auricularia auricula-judae
    • CrossRef PubMed
    • Linde, D., Coscolín, C., Liers, C., Hofrichter, M., Martínez, A.T. and Ruiz-Dueñas, F.J. (2014) Heterologous expression and physicochemical characterization of a fungal dye-decolorizing peroxidase from Auricularia auricula-judae. Protein Expr. Purif. 103, 28-37 CrossRef PubMed
    • (2014) Protein Expr. Purif. , vol.103 , pp. 28-37
    • Linde, D.1    Coscolín, C.2    Liers, C.3    Hofrichter, M.4    Martínez, A.T.5    Ruiz-Dueñas, F.J.6
  • 21
    • 79958856367 scopus 로고    scopus 로고
    • Identification of DypB from Rhodococcus jostii RHA1 as a lignin peroxidase
    • CrossRef PubMed
    • Ahmad, M., Roberts, J.N., Hardiman, E.M., Singh, R., Eltis, L.D. and Bugg, T. D. H. (2011) Identification of DypB from Rhodococcus jostii RHA1 as a lignin peroxidase. Biochemistry 50, 5096-5107 CrossRef PubMed
    • (2011) Biochemistry , vol.50 , pp. 5096-5107
    • Ahmad, M.1    Roberts, J.N.2    Hardiman, E.M.3    Singh, R.4    Eltis, L.D.5    Bugg, T.D.H.6
  • 22
    • 84891098502 scopus 로고    scopus 로고
    • Exploring bacterial lignin degradation
    • CrossRef PubMed
    • Brown, M.E. and Chang, M.C.Y. (2014) Exploring bacterial lignin degradation. Curr. Opin. Chem. Biol. 19, 1-7 CrossRef PubMed
    • (2014) Curr. Opin. Chem. Biol. , vol.19 , pp. 1-7
    • Brown, M.E.1    Chang, M.C.Y.2
  • 24
    • 0032573035 scopus 로고    scopus 로고
    • Two substrate interaction sites in lignin peroxidase revealed by site-directed mutagenesis
    • CrossRef PubMed
    • Doyle, W.A., Blodig, W., Veitch, N.C., Piontek, K. and Smith, A.T. (1998) Two substrate interaction sites in lignin peroxidase revealed by site-directed mutagenesis. Biochemistry 37, 15097-15105 CrossRef PubMed
    • (1998) Biochemistry , vol.37 , pp. 15097-15105
    • Doyle, W.A.1    Blodig, W.2    Veitch, N.C.3    Piontek, K.4    Smith, A.T.5
  • 25
    • 27644552270 scopus 로고    scopus 로고
    • Versatile peroxidase oxidation of high redox potential aromatic compounds: Site-directed mutagenesis, spectroscopic and crystallographic investigations of three long-range electron transfer pathways
    • CrossRef PubMed
    • Pérez-Boada, M., Ruiz-Dueñas, F.J., Pogni, R., Basosi, R., Choinowski, T., Martínez, M.J., Piontek, K. and Martínez, A.T. (2005) Versatile peroxidase oxidation of high redox potential aromatic compounds: site-directed mutagenesis, spectroscopic and crystallographic investigations of three long-range electron transfer pathways. J. Mol. Biol. 354, 385-402 CrossRef PubMed
    • (2005) J. Mol. Biol. , vol.354 , pp. 385-402
    • Pérez-Boada, M.1    Ruiz-Dueñas, F.J.2    Pogni, R.3    Basosi, R.4    Choinowski, T.5    Martínez, M.J.6    Piontek, K.7    Martínez, A.T.8
  • 26
    • 84875978674 scopus 로고    scopus 로고
    • In-silico assessment of protein-protein electron transfer. A case study: Cytochrome c peroxidase - cytochrome c
    • CrossRef PubMed
    • Wallrapp, F.H., Voityuk, A.A. and Guallar, V. (2013) In-silico assessment of protein-protein electron transfer. A case study: cytochrome c peroxidase - cytochrome c. PLoS Comput. Biol. 9, e1002990 CrossRef PubMed
    • (2013) PLoS Comput. Biol. , vol.9 , pp. e1002990
    • Wallrapp, F.H.1    Voityuk, A.A.2    Guallar, V.3
  • 27
    • 84876719258 scopus 로고    scopus 로고
    • Combined quantum mechanics/molecular mechanics (QM/MM) methods in computational enzymology
    • CrossRef PubMed
    • van der Kamp, M.W. and Mulholland, A.J. (2013) Combined quantum mechanics/molecular mechanics (QM/MM) methods in computational enzymology. Biochemistry 52, 2708-2728 CrossRef PubMed
    • (2013) Biochemistry , vol.52 , pp. 2708-2728
    • Van Der Kamp, M.W.1    Mulholland, A.J.2
  • 28
    • 77952674978 scopus 로고    scopus 로고
    • QM/MM methods: Looking inside heme proteins biochemisty
    • CrossRef PubMed
    • Guallar, V. and Wallrapp, F.H. (2010) QM/MM methods: looking inside heme proteins biochemisty. Biophys. Chem. 149, 1-11 CrossRef PubMed
    • (2010) Biophys. Chem. , vol.149 , pp. 1-11
    • Guallar, V.1    Wallrapp, F.H.2
  • 29
    • 34147107263 scopus 로고    scopus 로고
    • PELE: Protein Energy Landscape Exploration: A novel Monte Carlo based technique
    • CrossRef
    • Borrelli, K.W., Vitalis, A., Alcantara, R. and Guallar, V. (2005) PELE: Protein Energy Landscape Exploration: a novel Monte Carlo based technique. J. Chem. Theory Comput. 1, 1304-1311 CrossRef
    • (2005) J. Chem. Theory Comput. , vol.1 , pp. 1304-1311
    • Borrelli, K.W.1    Vitalis, A.2    Alcantara, R.3    Guallar, V.4
  • 30
    • 79958767629 scopus 로고    scopus 로고
    • Determination of a catalytic tyrosine in Trametes cervina lignin peroxidase with chemical modification techniques
    • CrossRef PubMed
    • Miki, Y., Ichinose, H. and Wariishi, H. (2011) Determination of a catalytic tyrosine in Trametes cervina lignin peroxidase with chemical modification techniques. Biotechnol. Lett. 33, 1423-1427 CrossRef PubMed
    • (2011) Biotechnol. Lett. , vol.33 , pp. 1423-1427
    • Miki, Y.1    Ichinose, H.2    Wariishi, H.3
  • 31
    • 58749105158 scopus 로고    scopus 로고
    • Mapping protein electron transfer pathways with QM/MM methods
    • CrossRef PubMed
    • Guallar, V. and Wallrapp, F. (2008) Mapping protein electron transfer pathways with QM/MM methods. J.R. Soc. Interface 5, S233-S239 CrossRef PubMed
    • (2008) J.R. Soc. Interface , vol.5 , pp. S233-S239
    • Guallar, V.1    Wallrapp, F.2
  • 32
    • 28844486080 scopus 로고    scopus 로고
    • EasySpin, a comprehensive software package for spectral simulation and analysis in EPR
    • CrossRef PubMed
    • Stoll, S. and Schweiger, A. (2006) EasySpin, a comprehensive software package for spectral simulation and analysis in EPR. J. Magn. Reson. 178, 42-55 CrossRef PubMed
    • (2006) J. Magn. Reson. , vol.178 , pp. 42-55
    • Stoll, S.1    Schweiger, A.2
  • 34
    • 79952163914 scopus 로고    scopus 로고
    • EPR parameters of amino acid radicals in P. eryngii versatile peroxidase and its W164Y variant computed at the QM/MM level
    • CrossRef PubMed
    • Bernini, C., Pogni, R., Ruiz-Dueñas, F.J., Martínez, A.T., Basosi, R. and Sinicropi, A. (2011) EPR parameters of amino acid radicals in P. eryngii versatile peroxidase and its W164Y variant computed at the QM/MM level. Phys. Chem. Chem. Phys. 13, 5078-5098 CrossRef PubMed
    • (2011) Phys. Chem. Chem. Phys. , vol.13 , pp. 5078-5098
    • Bernini, C.1    Pogni, R.2    Ruiz-Dueñas, F.J.3    Martínez, A.T.4    Basosi, R.5    Sinicropi, A.6
  • 35
    • 84875746568 scopus 로고    scopus 로고
    • Effects of the protein environment on the spectral properties of tryptophan radicals in Pseudomonas aeruginosa azurin
    • CrossRef PubMed
    • Bernini, C., Andruniow, T., Olivucci, M., Pogni, R., Basosi, R. and Sinicropi, A. (2013) Effects of the protein environment on the spectral properties of tryptophan radicals in Pseudomonas aeruginosa azurin. J. Am. Chem. Soc. 135, 4822-4833 CrossRef PubMed
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 4822-4833
    • Bernini, C.1    Andruniow, T.2    Olivucci, M.3    Pogni, R.4    Basosi, R.5    Sinicropi, A.6
  • 36
    • 79953889758 scopus 로고    scopus 로고
    • Chlorite dismutases, DyPs, and EfeB: 3 microbial heme enzyme families comprise the CDE structural superfamily
    • CrossRef PubMed
    • Goblirsch, B., Kurker, R.C., Streit, B.R., Wilmot, C.M. and Dubois, J.L. (2011) Chlorite dismutases, DyPs, and EfeB: 3 microbial heme enzyme families comprise the CDE structural superfamily. J. Mol. Biol. 408, 379-398 CrossRef PubMed
    • (2011) J. Mol. Biol. , vol.408 , pp. 379-398
    • Goblirsch, B.1    Kurker, R.C.2    Streit, B.R.3    Wilmot, C.M.4    Dubois, J.L.5
  • 37
    • 84897374057 scopus 로고    scopus 로고
    • Chlorite dismutases: A heme enzyme family for use in bioremediation and generation of molecular oxygen
    • CrossRef PubMed
    • Hofbauer, S., Schaffner, I., Furtmuller, P.G. and Obinger, C. (2014) Chlorite dismutases: a heme enzyme family for use in bioremediation and generation of molecular oxygen. Biotechnol. J. 9, 461-473 CrossRef PubMed
    • (2014) Biotechnol. J. , vol.9 , pp. 461-473
    • Hofbauer, S.1    Schaffner, I.2    Furtmuller, P.G.3    Obinger, C.4
  • 38
    • 12944305786 scopus 로고
    • Superfamily of plant, fungal and bacterial peroxidases
    • CrossRef
    • Welinder, K.G. (1992) Superfamily of plant, fungal and bacterial peroxidases. Curr. Opin. Struct. Biol. 2, 388-393 CrossRef
    • (1992) Curr. Opin. Struct. Biol. , vol.2 , pp. 388-393
    • Welinder, K.G.1
  • 39
  • 40
    • 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
    • CrossRef PubMed
    • Ruiz-Dueñas, F.J., Pogni, R., Morales, M., Giansanti, S., Mate, M.J., Romero, A., Martínez, M.J., Basosi, R. and Martínez, A.T. (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 CrossRef PubMed
    • (2009) J. Biol. Chem. , vol.284 , pp. 7986-7994
    • Ruiz-Dueñas, F.J.1    Pogni, R.2    Morales, M.3    Giansanti, S.4    Mate, M.J.5    Romero, A.6    Martínez, M.J.7    Basosi, R.8    Martínez, A.T.9
  • 41
    • 70349522119 scopus 로고    scopus 로고
    • Spectroscopic evidence for an engineered, catalytically active Trp radical that creates the unique reactivity of lignin peroxidase
    • CrossRef PubMed
    • Smith, A.T., Doyle, W.A., Dorlet, P. and Ivancich, A. (2009) Spectroscopic evidence for an engineered, catalytically active Trp radical that creates the unique reactivity of lignin peroxidase. Proc. Natl. Acad. Sci. U.S.A. 106, 16084-16089 CrossRef PubMed
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 16084-16089
    • Smith, A.T.1    Doyle, W.A.2    Dorlet, P.3    Ivancich, A.4
  • 42
  • 44
    • 0037117789 scopus 로고    scopus 로고
    • Molecular biology and structure-function of lignin-degrading heme peroxidases
    • CrossRef
    • Martínez, A.T. (2002) Molecular biology and structure-function of lignin-degrading heme peroxidases. Enzyme Microb. Technol. 30, 425-444 CrossRef
    • (2002) Enzyme Microb. Technol. , vol.30 , pp. 425-444
    • Martínez, A.T.1
  • 45
    • 67649786142 scopus 로고    scopus 로고
    • Substrate oxidation sites in versatile peroxidase and other basidiomycete peroxidases
    • CrossRef PubMed
    • Ruiz-Dueñas, F.J., Morales, M., García, E., Miki, Y., Martínez, M.J. and Martínez, A.T. (2009) Substrate oxidation sites in versatile peroxidase and other basidiomycete peroxidases. J. Exp. Bot. 60, 441-452 CrossRef PubMed
    • (2009) J. Exp. Bot. , vol.60 , pp. 441-452
    • Ruiz-Dueñas, F.J.1    Morales, M.2    García, E.3    Miki, Y.4    Martínez, M.J.5    Martínez, A.T.6
  • 46
    • 13844280911 scopus 로고    scopus 로고
    • EPR techniques for studying radical enzymes
    • CrossRef PubMed
    • Jeschke, G. (2005) EPR techniques for studying radical enzymes. Biochim. Biophys. Acta 1707, 91-102 CrossRef PubMed
    • (2005) Biochim. Biophys. Acta , vol.1707 , pp. 91-102
    • Jeschke, G.1
  • 47
    • 0035909806 scopus 로고    scopus 로고
    • Tryptophan and tyrosine radicals in ribonucleotide reductase: A comparative high-field EPR study at 94 GHz
    • CrossRef PubMed
    • Bleifuss, G., Kolberg, M., Potsch, S., Hofbauer, W., Bittl, R., Lubitz, W., Graslund, A., Lassmann, G. and Lendzian, F. (2001) Tryptophan and tyrosine radicals in ribonucleotide reductase: a comparative high-field EPR study at 94 GHz. Biochemistry 40, 15362-15368 CrossRef PubMed
    • (2001) Biochemistry , vol.40 , pp. 15362-15368
    • Bleifuss, G.1    Kolberg, M.2    Potsch, S.3    Hofbauer, W.4    Bittl, R.5    Lubitz, W.6    Graslund, A.7    Lassmann, G.8    Lendzian, F.9
  • 49
    • 84857912107 scopus 로고    scopus 로고
    • Redox properties of tyrosine and related molecules
    • CrossRef PubMed
    • Warren, J.J., Winkler, J.R. and Gray, H.B. (2012) Redox properties of tyrosine and related molecules. FEBS Lett. 586, 596-602 CrossRef PubMed
    • (2012) FEBS Lett. , vol.586 , pp. 596-602
    • Warren, J.J.1    Winkler, J.R.2    Gray, H.B.3
  • 50
    • 0032023777 scopus 로고    scopus 로고
    • Protein radicals in enzyme catalysis
    • CrossRef PubMed
    • Stubbe, J. and Der Donk, W.A. (1998) Protein radicals in enzyme catalysis. Chem. Rev. 98, 705-762 CrossRef PubMed
    • (1998) Chem. Rev. , vol.98 , pp. 705-762
    • Stubbe, J.1    Der Donk, W.A.2
  • 51
    • 84904528905 scopus 로고    scopus 로고
    • Engineering a fungal peroxidase that degrades lignin at very acidic pH
    • CrossRef
    • Fernández-Fueyo, E., Ruiz-Dueñas, F.J. and Martínez, A.T. (2014) Engineering a fungal peroxidase that degrades lignin at very acidic pH. Biotechnol. Biofuels 7, 114 CrossRef
    • (2014) Biotechnol. Biofuels , vol.7 , pp. 114
    • Fernández-Fueyo, E.1    Ruiz-Dueñas, F.J.2    Martínez, A.T.3
  • 53
    • 0013916008 scopus 로고
    • Reactivity toward N-bromosuccinimide of tryptophan in enzymes zymogens and inhibited enzymes
    • CrossRef PubMed
    • Spande, T.F., Green, N.M. and Witkop, B. (1966) Reactivity toward N-bromosuccinimide of tryptophan in enzymes zymogens and inhibited enzymes. Biochemistry 5, 1926-1933 CrossRef PubMed
    • (1966) Biochemistry , vol.5 , pp. 1926-1933
    • Spande, T.F.1    Green, N.M.2    Witkop, B.3
  • 54
    • 0013966806 scopus 로고
    • Tetranitromethane: A reagent for nitration of tyrosyl residues in proteins
    • CrossRef PubMed
    • Sokolovsky, M., Riordan, J.F. and Vallee, B.L. (1966) Tetranitromethane: a reagent for nitration of tyrosyl residues in proteins. Biochemistry 5, 3582-3589 CrossRef PubMed
    • (1966) Biochemistry , vol.5 , pp. 3582-3589
    • Sokolovsky, M.1    Riordan, J.F.2    Vallee, B.L.3
  • 55
    • 84870381055 scopus 로고    scopus 로고
    • Two oxidation sites for low redox-potential substrates: A directed mutagenesis, kinetic and crystallographic study on Pleurotus eryngii versatile peroxidase
    • CrossRef PubMed
    • Morales, M., Mate, M.J., Romero, A., Martínez, M.J., Martínez, A.T. and Ruiz-Dueñas, F.J. (2012) Two oxidation sites for low redox-potential substrates: a directed mutagenesis, kinetic and crystallographic study on Pleurotus eryngii versatile peroxidase. J. Biol. Chem. 287, 41053-41067 CrossRef PubMed
    • (2012) J. Biol. Chem. , vol.287 , pp. 41053-41067
    • Morales, M.1    Mate, M.J.2    Romero, A.3    Martínez, M.J.4    Martínez, A.T.5    Ruiz-Dueñas, F.J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.