CoChat
Sign Up
Cited by 527

The DOI matches its Crossref record.

New and classic families of secreted fungal heme peroxidases

Hofrichter, Martin, Ullrich, René, Pecyna, Marek J., Liers, Christiane, Lundell, Taina·2010·Applied Microbiology and Biotechnology
DOI 10.1007/s00253-010-2633-0
Open this paper in CoChat — free account

Abstract

Heme-containing peroxidases secreted by fungi are a fascinating group of biocatalysts with various ecological and biotechnological implications. For example, they are involved in the biodegradation of lignocelluloses and lignins and participate in the bioconversion of other diverse recalcitrant compounds as well as in the natural turnover of humic substances and organohalogens. The current review focuses on the most recently discovered and novel types of heme-dependent peroxidases, aromatic peroxygenases (APOs), and dye-decolorizing peroxidases (DyPs), which catalyze remarkable reactions such as peroxide-driven oxygen transfer and cleavage of anthraquinone derivatives, respectively, and represent own separate peroxidase superfamilies. Furthermore, several aspects of the "classic" fungal heme-containing peroxidases, i.e., lignin, manganese, and versatile peroxidases (LiP, MnP, and VP), phenol-oxidizing peroxidases as well as chloroperoxidase (CPO), are discussed against the background of recent scientific developments.

Overview

Integrity signals

Registry

Crossref · 10.1007/s00253-010-2633-0

Cites

Statistics

Recomputing p-values needs the paper’s full text.

Verification

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Citations

Cites

No references could be resolved yet.

Research works printed but not linked: 242

  1. Alvarado B, Torres E (2009) Recents patents in the use of peroxidases. Recent Pat Biotechnol 3:88–102 · DOI
  2. Anh DH, Ullrich R, Benndorf D, Svatos A, Muck A, Hofrichter M (2007) The coprophilous mushroom Coprinus radians secretes a haloperoxidase that catalyzes aromatic peroxygenation. Appl Environ Microbiol 73:5477–5485 · DOI
  3. Aranda E, Kinne M, Kluge M, Ullrich R, Hofrichter M (2009) Conversion of dibenzothiophene by the mushrooms Agrocybe aegerita and Coprinellus radians and their extracellular peroxygenases. Appl Microbiol Biotechnol 82:1057–1066 · DOI
  4. Aranda E, Ullrich R, Hofrichter M (2010) Conversion of polycyclic aromatic hydrocarbons, methyl naphthalenes and dibenzofuran by two fungal peroxygenases. Biodegradation 21:267–281 · DOI
  5. Ayala M, Robledo NR, Lopez-Munguia A, Vazquez-Duhalt R (2000) Substrate specificity and ionization potential in chloroperoxidase-catalyzed oxidation of diesel fuel. Environ Sci Technol 34:2804–2809 · DOI
  6. Ayala M, Roman R, Vazquez-Duhalt R (2007) A catalytic approach to estimate the redox potential of heme-peroxidases. Biochem Biophys Res Commun 357:804–808 · DOI
  7. Ayala M, Pickard MA, Vazquez-Duhalt R (2008) Fungal enzymes for environmental purposes, a molecular biology challenge. J Mol Microbiol Biotechnol 15:172–180 · DOI
  8. Azevedo AM, Martins VC, Prazeres DM, Vojinovic V, Cabral JM, Fonseca LP (2003) Horseradish peroxidase: a valuable tool in biotechnology. Biotechnol Annu Rev 9:199–247 · DOI · Paper page
  9. Baciocchi E, Bietti M, Gerini MF, Lanzalunga O (2002) The mediation of veratryl alcohol in oxidations promoted by lignin peroxidase: the lifetime of veratryl alcohol radical cation. Biochem Biophys Res Commun 293:832–835 · DOI
  10. Baldrian P (2006) Fungal laccases—occurrence and properties. FEMS Microbiol Rev 30:215–242 · DOI
  11. Banci L, Ciofi-Baffoni S, Tien M (1999) Lignin and Mn peroxidase-catalyzed oxidation of phenolic lignin oligomers. Biochemistry 38:3205–3210 · DOI
  12. Bengtson P, Bastviken D, de Boer W, Oberg G (2009) Possible role of reactive chlorine in microbial antagonism and organic matter chlorination in terrestrial environments. Environ Microbiol 11:1330–1339 · DOI
  13. Blanke SR, Yi S, Hager LP (1989) Development of semi-continuous and continuous flow bioreactors for the high level production of chloroperoxidase. Biotechnol Lett 11:769–774 · DOI
  14. 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 · DOI
  15. Bond AM, Fleming BD, Martin LL (2007) The electrochemistry of cytochrome P450. In: Sigel A, Sigel H, Sigel RKO (eds) Metal ions in life sciences, 1st edn. John Wiley & Sons Ltd, Chichester, pp 127–155
  16. Borole AP, Davison BH (2007) Techno-economic analysis of biocatalytic processes for production of alkene epoxides. Appl Biochem Biotechnol 137–140:437–449
  17. Bumpus JA (1989) Biodegradation of polycyclic hydrocarbons by Phanerochaete chrysosporium. Appl Environ Microbiol 55:154–158 · DOI
  18. Cai D, Tien M (1992) Kinetic studies on the formation and decomposition of compounds II and III. Reactions of lignin peroxidase with H2O2. J Biol Chem 267:11149–11155 · DOI
  19. Cartron ML, Mitchell SA, Woodhall MR, Andrews SC, Watson KA (2007) Preliminary X-ray diffraction analysis of YcdB from Escherichia coli: a novel haem-containing and Tat-secreted periplasmic protein with a potential role in iron transport. Acta Crystallogr F Struct Biol Cryst Commun 63:37–41 · DOI
  20. Casella L, Poli S, Gullotti M, Selvaggini C, Beringhelli T, Marchesini A (1994) The chloroperoxidase-catalyzed oxidation of phenols. Mechanism, selectivity, and characterization of enzyme-substrate complexes. Biochemistry 33:6377–6386 · DOI
  21. Chang HC, Holland RD, Bumpus JA, Churchwell MI, Doerge DR (1999) Inactivation of Coprinus cinereus peroxidase by 4-chloroaniline during turnover: comparison with horseradish peroxidase and bovine lactoperoxidase. Chemico-Biol Int 123:197–217 · DOI
  22. Chiang R, Rand-Meir T, Makino R, Hager LP (1976) Compound X. An intermediate in enzymatic halogenation. J Biol Chem 251:6340–6346 · DOI
  23. 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 cβ of tryptophan 171: a novel radical site formed during the redox cycle. J Mol Biol 286:809–827 · DOI
  24. Conesa A, Punt PJ, van Luijk N, van den Hondel CA (2001) The secretion pathway in filamentous fungi: a biotechnological view. Fungal Genet Biol 33:155–171 · DOI
  25. Conesa A, Punt PJ, van den Hondel CA (2002) Fungal peroxidases: molecular aspects and applications. J Biotechnol 93:143–158 · DOI
  26. Cullen D (1997) Recent advances on the molecular genetics of ligninolytic fungi. J Biotechnol 53:273–289 · DOI
  27. Dai L, Klibanov AM (2000) Peroxidase-catalyzed asymmetric sulfoxidation in organic solvents versus in water. Biotechnol Bioeng 70:353–357 · DOI
  28. Dau AH (2008) Novel extracellular haloperoxidase-peroxygenases from the coprophilous fungi Coprinus radians and Coprinus verticillatus: production, purification and biochemical characterization. Ph.D. Thesis (dissertation), Unit of Environmental Biotechnology, International Graduate School of Zittau (Germany)
  29. Dawson JH (1988) Probing structure-function relations in heme-containing oxygenases and peroxidases. Science 240:433–439 · DOI
  30. de Hoog HM, Nallani M, Cornelissen JJ, Rowan AE, Nolte RJ, Arends IW (2009) Biocatalytic oxidation by chloroperoxidase from Caldariomyces fumago in polymersome nanoreactors. Org Biomol Chem 7:4604–4610 · DOI
  31. Dingler C, Ladner W, Krei GA, Cooper BS, Hauer B (1996) Preparation of (R)-2-(4-hydroxyphenoxy)propionic acid by biotransformation. Pestic Sci 46:33–53 · DOI
  32. 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 · DOI
  33. Dunford HB (1991) Horseradish peroxidase: structure and kinetic properties. In: Everse J, Everse KE, Grisham MB (eds) Peroxidases in chemistry and biology, 1st edn. CRC Press, Boca Raton, Ann Arbor, Boston, pp 1–24
  34. Dunford HB (1999) Heme peroxidases, 1st edn. Wiley-VCH, New York
  35. Everse J, Everse KE, Grisham MB (1991a) Peroxidases in chemistry and biology. 1st edn., vol. I, 1st edn. CRC Press, Boca Raton, Ann Arbor, Boston
  36. Everse J, Everse KE, Grisham MB (1991b) Peroxidases in chemistry and biology. 1st edn., vol. II. CRC Press, Boca Raton, Ann Arbor, Boston
  37. Faraco V, Piscitelli A, Sannia G, Giardina P (2007) Identification of a new member of the dye-decolorizing peroxidase family from Pleurotus ostreatus. World J Microbiol Biotechnol 23:889–893 · DOI
  38. Ferreira P, Hernández-Ortega A, Herguedas B, Martínez AT, Medina M (2009) Aryl-alcohol oxidase involved in lignin degradation: a mechanistic study based on steady and pre-steady state kinetics and primary and solvent isotope effects with two alcohol substrates. J Biol Chem 284:28840–28847
  39. Fleischmann P, Zorn H (2008) Enzymic pathways for formation of carotenoid cleavage products. In: Britton G, Liaaen-Jensen S, Pfander H (eds) Carotenoids: natural functions, 1st edn. Birkhäuser, Basel, pp 341–366 · DOI
  40. Fleischmann A, Darsow M, Degtyarenko K, Fleischmann W, Boyce S, Axelsen KB, Bairoch A, Schomburg D, Tipton KF, Apweiler R (2004) IntEnz, the integrated relational enzyme database. Nucleic Acids Res 32:D434–D437 · DOI
  41. Fournier D, Halasz A, Spain J, Spanggord RJ, Bottaro JC, Hawari J (2004) Biodegradation of the hexahydro-1, 3, 5-trinitro-1, 3, 5-triazine ring cleavage product 4-nitro-2, 4-diazabutanal by Phanerochaete chrysosporium. Appl Environ Microbiol 70:1123–1128 · DOI
  42. Gazarian IG, Lagrimini LM (1996) Purification and unusual kinetic properties of a tobacco anionic peroxidase. Phytochemistry 41:1029–1034 · DOI
  43. Gazarian IG, Lagrimini LM (1998) Anaerobic stopped-flow studies of indole-3-acetic acid oxidation by dioxygen catalysed by horseradish C and anionic tobacco peroxidase at neutral pH: catalase effect. Biophys Chem 72:231–237 · DOI
  44. Gazarian IG, Lagrimini LM, Mellon FA, Naldrett MJ, Ashby GA, Thorneley RN (1998) Identification of skatolyl hydroperoxide and its role in the peroxidase-catalysed oxidation of indol-3-yl acetic acid. Biochem J 333(Pt1):223–232 · DOI
  45. Geigert J, Lee TD, Dalietos DJ, Hirano DS, Neidleman SL (1986) Epoxidation of alkenes by chloroperoxidase catalysis. Biochem Biophys Res Commun 136:778–782 · DOI
  46. Gold MH, Youngs HL, Gelpke MD (2000) Manganese peroxidase. Met Ions Biol Syst 37:559–586
  47. Gonzalez FJ (2005) Role of cytochromes P450 in chemical toxicity and oxidative stress: studies with CYP2E1. Mutat Res 569:101–110 · DOI · Paper page
  48. Grey CE, Rundbäck F, Adlercreutz P (2008) Improved operational stability of chloroperoxidase through use of antioxidants. J Biotechnol 135:196–201 · DOI
  49. Hager LP, Morris DR, Brown FS, Eberwein H (1966) Chloroperoxidase. II. Utilization of halogen anions. J Biol Chem 241:1769–1777 · DOI
  50. Hammel KE, Cullen D (2008) Role of fungal peroxidases in biological ligninolysis. Curr Opin Plant Biol 11:349–355 · DOI
  51. Hammel KE, Moen MA (1991) Depolymerization of a synthetic lignin in vitro by lignin peroxidase. Enzyme Microb Technol 13:15–18 · DOI
  52. Hammel KE, Kalyanaraman B, Kirk TK (1986) Oxidation of polycyclic aromatic hydrocarbons and dibenzo[p]-dioxins by Phanerochaete chrysosporium ligninase. J Biol Chem 261:16948–16952 · DOI
  53. Hammel KE, Jensen KA Jr, Mozuch MD, Landucci LL, Tien M, Pease EA (1993) Ligninolysis by a purified lignin peroxidase. J Biol Chem 268:12274–12281 · DOI
  54. Hanano A, Burcklen M, Flenet M, Ivancich A, Louwagie M, Garin J, Blee E (2006) Plant seed peroxygenase is an original heme-oxygenase with an EF-hand calcium binding motif. J Biol Chem 281:33140–33151 · DOI
  55. Hatakka A (2001) Biodegradation of lignin. In: Hofrichter M, Steinbüchel A (eds) Biopolymers: lignin, humic substances and coal, 1st edn. Wiley-VCH, Weinheim, pp 129–180
  56. Hatakka A, Hammel KE (2010) Fungal biodegradation of lignocelluloses. In: Hofrichter M (ed.) The Mycota, X, Industrial applications, 2nd edn. Springer, Berlin Heidelberg New York (in press) · DOI
  57. Hatakka A, Lundell T, Hofrichter M, Maijala P (2003) Manganese peroxidase and its role in the degradation of wood lignin. In: Mansfield SD, Saddler JN (eds) Applications of enzymes to lignocellulosics, ACS Symposium Series 855. American Chemical Society, Washington DC, pp 230–243 · DOI
  58. Hildén K, Martinez AT, Hatakka A, Lundell T (2005) The two manganese peroxidases Pr-MnP2 and Pr-MnP3 of Phlebia radiata, a lignin-degrading basidiomycete, are phylogenetically and structurally divergent. Fungal Genet Biol 42:403–419 · DOI
  59. Hofrichter M (2002) Review: lignin conversion by manganese peroxidase (MnP). Enzyme Microb Technol 30:454–466 · DOI
  60. Hofrichter M, Ullrich R (2006) Heme-thiolate haloperoxidases: versatile biocatalysts with biotechnological and environmental significance. Appl Microbiol Biotechnol 71:276–288 · DOI
  61. Hofrichter M, Ullrich R (2010) New trends in fungal biooxidation. In: Hofrichter M (ed.) The Mycota, X, Industrial applications, 2nd edn. Springer, Berlin Heidelberg New York (in press) · DOI
  62. Hofrichter M, Ziegenhagen D, Vares T, Friedrich M, Jager MG, Fritsche W, Hatakka A (1998) Oxidative decomposition of malonic acid as basis for the action of manganese peroxidase in the absence of hydrogen peroxide. FEBS Lett 434:362–366 · DOI
  63. Hofrichter M, Vares T, Kalsi M, Galkin S, Scheibner K, Fritsche W, Hatakka A (1999) Production of manganese peroxidase and organic acids and mineralization of 14C-labelled lignin (14C-DHP) during solid-state fermentation of wheat straw with the white rot fungus Nematoloma frowardii. Appl Environ Microbiol 65:1864–1870 · DOI
  64. Hofrichter M, Lundell T, Hatakka A (2001) Conversion of milled pine wood by manganese peroxidase from Phlebia radiata. Appl Environ Microbiol 67:4588–4593 · DOI
  65. Hofrichter M, Ullrich R, Pecyna M, Kinne M, Kluge M, Aranda E, Liers C, Poraj-Kobielska M, Gröbe G, Scheibner K, Bittner B, Piontek K, Schubert R, Hammel K (2009) Aromatic peroxygenases from mushrooms: extracellular heme-thiolate proteins of a new enzyme sub-subclass? In: Shoun H, Ohkawa H (eds), 16th International Conference on Cytochrome P450 (Nago, Okinawa, Japan), Medimond (International Proceedings), Bologna, (Italy), pp. 83–88
  66. Horn A (2009) The use of a novel peroxidase from the basidiomycete Agrocybe aegerita as an example of enatioselective sulfoxidation (Der Einsatz einer neuartigen Peroxidase des Basidiomyceten Agrocybe aegerita am Beispiel der enatioselektiven Sulfoxidation). Dissertation, University of Rostock
  67. Houborg K, Harris P, Poulsen JC, Schneider P, Svendsen A, Larsen S (2003) The structure of a mutant enzyme of Coprinus cinereus peroxidase provides an understanding of its increased thermostability. Acta Crystallogr D Biol Crystallogr 59:997–1003 · DOI
  68. Huang Q, Huang Q, Pinto RA, Griebenow K, Schweitzer-Stenner R, Weber WJ Jr (2005) Inactivation of horseradish peroxidase by phenoxyl radical attack. J Am Chem Soc 127:1431–1437 · DOI
  69. Huang ST, Tzean SS, Tsai BY, Hsieh HJ (2009) Cloning and heterologous expression of a novel ligninolytic peroxidase gene from poroid brown-rot fungus Antrodia cinnamomea. Microbiology 155:424–433 · DOI
  70. Husain Q, Husain M, Kulshrestha Y (2009) Remediation and treatment of organopollutants mediated by peroxidases: a review. Crit Rev Biotechnol 29:94–119 · DOI
  71. Ikehata K, Buchanan ID (2002) Screening of Coprinus species for the production of extracellular peroxidase and evaluation of the enzyme for the treatment of aqueous phenol. Environ Technol 23:1355–1367 · DOI
  72. Ishimaru A, Yamazaki I (1977) Hydroperoxide-dependent hydroxylation involving "H2O2-reducible hemoprotein" in microsomes of pea seeds. A new type enzyme acting on hydroperoxide and a physiological role of seed lipoxygenase. J Biol Chem 252:6118–6124 · DOI
  73. Johansson T, Nyman PO (1993) Isozymes of lignin peroxidase and manganese(II) peroxidase from the white-rot basidiomycete Trametes versicolor. I. Isolation of enzyme forms and characterization of physical and catalytic properties. Arch Biochem Biophys 300:49–56 · DOI
  74. Jongbloed JD, Grieger U, Antelmann H, Hecker M, Nijland R, Bron S, van Dijl JM (2004) Two minimal Tat translocases in Bacillus. Mol Microbiol 54:1319–1325 · DOI
  75. Joo H, Lin Z, Arnold FH (1999) Laboratory evolution of peroxide-mediated cytochrome P450 hydroxylation. Nature 399:670–673 · DOI
  76. Joshi DK, Gold MH (1993) Degradation of 2, 4, 5-trichlorophenol by the lignin-degrading basidiomycete Phanerochaete chrysosporium. Appl Environ Microbiol 59:1779–1785 · DOI
  77. Juliána MC, Aceroa J, Salazara O, Keijerb J, Rubio V (1999) Mating type-correlated molecular markers and demonstration of heterokaryosis in the phytopathogenic fungus Thanatephorus cucumeris (Rhizoctonia solani) AG 1-IC by AFLP DNA fingerprinting analysis. J Biotech 67:49–56 · DOI
  78. Jung D, Paradiso M, Wallacher D, Brandt A, Hartmann M (2009) Formation of cross-linked chloroperoxidase aggregates in the pores of mesocellular foams: characterization by SANS and catalytic properties. ChemSusChem 2:161–164 · DOI
  79. Kauffmann C, Petersen BR, Bjerrum MJ (1999) Enzymatic removal of phenols from aqueous solutions by Coprinus cinereus peroxidase and hydrogen peroxide. J Biotechnol 73:71–74 · DOI
  80. Kaup BA, Ehrich K, Pescheck M, Schrader J (2008) Microparticle-enhanced cultivation of filamentous microorganisms: increased chloroperoxidase formation by Caldariomyces fumago as an example. Biotechnol Bioeng 99:491–498 · DOI
  81. Kersten PJ, Kalyanaraman B, Hammel KE, Reinhammar B, Kirk TK (1990) Comparison of lignin peroxidase, horseradish peroxidase and laccase in the oxidation of methoxybenzenes. Biochem J 268:475–480 · DOI
  82. Kim SJ, Shoda M (1999a) Decolorization of molasses and a dye by a newly isolated strain of the fungus Geotrichum candidum Dec 1. Biotechnol Bioeng 62:114–119 · DOI
  83. Kim SJ, Shoda M (1999b) Purification and characterization of a novel peroxidase from Geotrichum candidum Dec 1 involved in decolorization of dyes. Appl Environ Microbiol 65:1029–1035 · DOI · Paper page
  84. Kim SJ, Ishikawa K, Hirai M, Shoda M (1995) Characteristics of a newly isolated fungus, Geotrichum candidum Dec 1, which decolorizes various dyes. J Ferment Bioeng 79:601–607 · DOI
  85. Kim YH, An ES, Park SY, Lee J-O, Kim JH, Song BK (2007) Polymerization of bisphenol a using Coprinus cinereus peroxidase (CiP) and its application as a photoresist resin. J Mol Cat B 44:149–154 · DOI
  86. Kim HS, Cho DH, Won K, Kim YH (2009) Inactivation of Coprinus cinereus peroxidase during the oxidation of various phenolic compounds originated from lignin. Enzyme Microb Technol 45:150–155 · DOI
  87. Kinne M, Ullrich R, Hammel KE, Hofrichter M (2008) Regioselective preparation of (R)-2-(4-Hydroxyphenoxy)propionic acid with a fungal peroxygenase. Tetrahedron Lett 49:5950–5953 · DOI
  88. Kinne M, Poraj-Kobielska M, Aranda E, Ullrich R, Hammel KE, Scheibner K, Hofrichter M (2009a) Regioselective preparation of 5-hydroxypropranolol and 4′-hydroxydiclofenac with a fungal peroxygenase. Bioorg Med Chem Lett 19:3085–3087 · DOI
  89. Kinne M, Poraj-Kobielska M, Ralph SA, Ullrich R, Hofrichter M, Hammel KE (2009b) Oxidative cleavage of diverse ethers by an extracellular fungal peroxygenase. J Biol Chem 284:29343–29349 · DOI
  90. Kinne M, Zeisig C, Ullrich R, Kayser G, Hammel KE, Hofrichter M (2010) Stepwise oxygenations of toluene and 4-nitrotoluene by a fungal peroxygenase. Biochem Byophys Res Comm (accepted) · DOI
  91. Kjalke M, Andersen MB, Schneider P, Christensen B, Schulein M, Welinder KG (1992) Comparison of structure and activities of peroxidases from Coprinus cinereus, Coprinus macrorhizus and Arthromyces ramosus. Biochim Biophys Acta 1120:248–256 · DOI
  92. Klebanoff SJ (2005) Myeloperoxidase: friend and foe. J Leukoc Biol 77:598–625 · DOI · Paper page
  93. Klibanov AM (2003) Asymmetric enzymatic oxidoreductions in organic solvents. Curr Opin Biotechnol 14:427–431 · DOI
  94. Kluge MG, Ullrich R, Scheibner K, Hofrichter M (2007) Spectrophotometric assay for detection of aromatic hydroxylation catalyzed by fungal haloperoxidase-peroxygenase. Appl Microbiol Biotechnol 75:1473–1478 · DOI
  95. Kluge M, Ullrich R, Dolge C, Scheibner K, Hofrichter M (2009) Hydroxylation of naphthalene by aromatic peroxygenase from Agrocybe aegerita proceeds via oxygen transfer from H2O2 and intermediary epoxidation. Appl Microbiol Biotechnol 81:1071–1076 · DOI
  96. Kolkman MA, van der Ploeg R, Bertels M, van Dijk M, van der Laan J, van Dijl JM, Ferrari E (2008) The twin-arginine signal peptide of Bacillus subtilis YwbN can direct either Tat- or Sec-dependent secretion of different cargo proteins: secretion of active subtilisin via the B. subtilis Tat pathway. Appl Environ Microbiol 74:7507–7513 · DOI
  97. Koskiniemi H, Metsa-Ketela M, Dobritzsch D, Kallio P, Korhonen H, Mantsala P, Schneider G, Niemi J (2007) Crystal structures of two aromatic hydroxylases involved in the early tailoring steps of angucycline biosynthesis. J Mol Biol 372:633–648 · DOI
  98. Kuan IC, Tien M (1993) Stimulation of Mn peroxidase activity: a possible role for oxalate in lignin biodegradation. Proc Natl Acad Sci U S A 90:1242–1246 · DOI
  99. Kühnel K, Blankenfeldt W, Terner J, Schlichting I (2006) Crystal structures of chloroperoxidase with its bound substrates and complexed with formate, acetate, and nitrate. J Biol Chem 281:23990–23998 · DOI
  100. Kunishima N, Fukuyama K, Matsubara H, Hatanaka H, Shibano Y, Amachi T (1994) Crystal structure of the fungal peroxidase from Arthromyces ramosus at 1.9 A resolution. Structural comparisons with the lignin and cytochrome c peroxidases. J Mol Biol 235:331–344 · DOI
  101. Lambeir AM, Dunford HB (1983) A kinetic and spectral study of the alkaline transitions of chloroperoxidase. Arch Biochem Biophys 220:549–556 · DOI
  102. Lankinen P, Hildén K, Aro N, Salkinoja-Salonen M, Hatakka A (2005) Manganese peroxidase of Agaricus bisporus: grain bran-promoted production and gene characterization. Appl Microbiol Biotechnol 66:401–407 · DOI
  103. Larrondo L, Gonzalez A, Perez Acle T, Cullen D, Vicuna R (2005) The nop gene from Phanerochaete chrysosporium encodes a peroxidase with novel structural features. Biophys Chem 116:167–173 · DOI
  104. Leak DJ, Sheldon RA, Woodley JM, Adlercreutz P (2009) Biocatalysts for selective introduction of oxygen. Biocat Biotrans 27:1–26 · DOI
  105. Libby RD, Thomas JA, Kaiser LW, Hager LP (1982) Chloroperoxidase halogenation reactions. Chemical versus enzymic halogenating intermediates. J Biol Chem 257:5030–5037 · DOI
  106. Liers C, Ullrich R, Kinne M, Pecyna M, Kluge M, Aranda E, Scheibner K, Hofrichter M (2009) Oxidation of non-phenolic lignin model compounds by novel fungal peroxidases. Proceedings book of the INTB Conference on "Biotechnological Functionalisation of Advanced Fibre Reinforced Composites". University of Ghent, Ghent, pp. 238–243
  107. Liers C, Bobeth C, Pecyna M, Ullrich R, 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 · DOI
  108. Littlechild J (1999) Haloperoxidases and their role in biotransformation reactions. Curr Opin Chem Biol 3:28–34 · DOI
  109. Liu JZ, Wang M (2007) Improvement of activity and stability of chloroperoxidase by chemical modification. BMC Biotechnol 7:23 · DOI
  110. Liu KK-C, Wong C-H (1992) Enzymatic halohydration of glycals. J Org Chem 57:3748–3750 · DOI
  111. Longoria A, Tinoco R, Vázquez-Duhalt R (2008) Chloroperoxidase-mediated transformation of highly halogenated monoaromatic compounds. Chemosphere 72:485–490 · DOI
  112. Longoria AM, Hu H, Vazquez-Duhalt R (2009) Enzymatic synthesis of semiconductor polymers by chloroperoxidase of Caldariomyces fumago. Appl Biochem Biotechnol. doi: 10.1007/s12010-009-8805-7 · DOI
  113. Lundell T (1993) Ligninolytic system of the white-rot fungus Phlebia radiata: Lignin model compound studies. Ph.D. Thesis (dissertation), Department of Applied Chemistry and Microbiology, University of Helsinki (Finland)
  114. Lundell T, Schoemaker H, Hatakka A, Brunow G (1993a) New mechanism of the Cα-Cβ cleavage in non-phenolic arylglycerol β-aryl ether lignin substructures catalyzed by lignin peroxidase. Holzforschung 47:219–224 · DOI
  115. Lundell T, Wever R, Floris R, Harvey P, Hatakka A, Brunow G, Schoemaker H (1993b) Lignin peroxidase L3 from Phlebia radiata. Pre-steady-state and steady-state studies with veratryl alcohol and a non-phenolic lignin model compound 1-(3, 4-dimethoxyphenyl)-2-(2-methoxyphenoxy)propane-1, 3-diol. Eur J Biochem 211:391–402 · DOI
  116. Lundell TK, Mäkelä MR, Hildén K (2010) Lignin-modifying enzymes in filamentous basidiomycetes: ecological, functional and phylogenetic review. J Basic Microbiol 50:1–16 · DOI
  117. Makris TM, Denisov I, Schlichting I, Sligar SG (2005) Activation of molecular oxygen by cytochrome P450. In: Ortiz De Montellano PR (ed) Cytochrome P450 - structure, mechanism and biochemistry, 3rd edn. Kluwer Academic/Plenum Publishers, New York, pp 149–182 · DOI
  118. Manoj KM (2006) Chlorinations catalyzed by chloroperoxidase occur via diffusible intermediate(s) and the reaction components play multiple roles in the overall process. Biochim Biophys Acta 1764:1325–1339 · DOI
  119. Manoj KM, Hager LP (2006) A colorimetric method for detection and quantification of chlorinating activity of hemeperoxidases. Anal Biochem 348:84–86 · DOI
  120. Manoj KM, Hager LP (2008) Chloroperoxidase, a janus enzyme. Biochemistry 47:2997–3003 · DOI
  121. Manoj KM, Lakner FJ, Hager LP (2000) Epoxidation of indene by chloroperoxidase. J Mol Catal B Enzym 9:107–111 · DOI
  122. Marjamaa K, Hildén K, Kukkola E, Lehtonen M, Holkeri H, Haapaniemi P, Koutaniemi S, Teeri TH, Fagerstedt K, Lundell T (2006) Cloning, characterization and localization of three novel class III peroxidases in lignifying xylem of Norway spruce (Picea abies). Plant Mol Biol 61:719–732 · DOI
  123. Martin F, Aerts A, Ahrén D, Brun A, Danchin EG, Duchaussoy F, Gibon J, Kohler A, Lindquist E, Pereda V, Salamov A, Shapiro HJ, Wuyts J, Blaudez D, Buée M, Brokstein P, Canbäck B, Cohen D, Courty PE, Coutinho PM, Delaruelle C, Detter JC, Deveau A, DiFazio S, Duplessis S, Fraissinet-Tachet L, Lucic E, Frey-Klett P, Fourrey C, Feussner I, Gay G, Grimwood J, Hoegger PJ, Jain P, Kilaru S, Labbé J, Lin YC, Legué V, Le Tacon F, Marmeisse R, Melayah D, Montanini B, Muratet M, Nehls U, Niculita-Hirzel H, Oudot-Le Secq MP, Peter M, Quesneville H, Rajashekar B, Reich M, Rouhier N, Schmutz J, Yin T, Chalot M, Henrissat B, Kües U, Lucas S, Van de Peer Y, Podila GK, Polle A, Pukkila PJ, Richardson PM, Rouzé P, Sanders IR, Stajich JE, Tunlid A, Tuskan G, Grigoriev IV (2008) The genome of Laccaria bicolor provides insights into mycorrhizal symbiosis. Nature 452:88–92 · DOI
  124. Martínez AT (2002) Molecular biology and structure-function of lignin-degrading heme peroxidases. Enzyme Microb Technol 30:425–444 · DOI
  125. Martínez AT (2007) High redox potential peroxidases. In: Polaina J, MacCabe AP (eds) Industrial enzymes: structure, function and applications, 1st edn. Springer-Verlag, Berlin, pp 475–486
  126. Martínez AT, Speranza M, Ruiz-Dueñas FJ, Ferreira P, Camarero S, Guillen F, Martínez MJ, Gutiérrez A, del Río JC (2005) Biodegradation of lignocellulosics: microbial, chemical, and enzymatic aspects of the fungal attack of lignin. Int Microbiol 8:195–204
  127. Martínez AT, Ruiz-Dueñas FJ, Martínez MJ, Del Rio JC, Gutierrez A (2009) Enzymatic delignification of plant cell wall: from nature to mill. Curr Opin Biotechnol 20:348–357 · DOI
  128. Martinez D, Larrondo LF, Putnam N, Gelpke MD, Huang K, Chapman J, Helfenbein KG, Ramaiya P, Detter JC, Larimer F, Coutinho PM, Henrissat B, Berka R, Cullen D, Rokhsar D (2004) Genome sequence of the lignocellulose degrading fungus Phanerochaete chrysosporium strain RP78. Nat Biotechnol 22:695–700 · DOI
  129. Martinez D, Challacombe J, Morgenstern I, Hibbett D, Schmoll M, Kubicek CP, Ferreira P, Ruiz-Duenas FJ, Martinez AT, Kersten P, Hammel KE, Vanden Wymelenberg A, Gaskell J, Lindquist E, Sabat G, Bondurant SS, Larrondo LF, Canessa P, Vicuna R, Yadav J, Doddapaneni H, Subramanian V, Pisabarro AG, Lavín JL, Oguiza JA, Master E, Henrissat B, Coutinho PM, Harris P, Magnuson JK, Baker SE, Bruno K, Kenealy W, Hoegger PJ, Kües U, Ramaiya P, Lucas S, Salamov A, Shapiro H, Tu H, Chee CL, Misra M, Xie G, Teter S, Yaver D, James T, Mokrejs M, Pospisek M, Grigoriev IV, Brettin T, Rokhsar D, Berka R, Cullen D (2009) Genome, transcriptome, and secretome analysis of wood decay fungus Postia placenta supports unique mechanisms of lignocellulose conversion. Proc Natl Acad Sci U S A 106:1954–1959 · DOI
  130. Martínez MJ, Böckle B, Camarero S, Guillén F, Martínez AT (1996) MnP isoenzymes produced by two Pleurotus species in liquid culture and during wheat-straw solid-state fermentation ACS Symposium Series 655. American Chemical Society, Washington DC, pp 183–196
  131. Mester T, Field JA (1998) Characterization of a novel manganese peroxidase-lignin peroxidase hybrid isozyme produced by Bjerkandera species strain BOS55 in the absence of manganese. J Biol Chem 273:15412–15417 · DOI
  132. Michels J, Gottschalk G (1994) Inhibition of the lignin peroxidase of Phanerochaete chrysosporium by hydroxylamino-dinitrotoluene, an early intermediate in the degradation of 2, 4, 6-trinitrotoluene. Appl Environ Microbiol 60:187–194 · DOI
  133. Miki K, Renganathan V, Gold MH (1986) Mechanism of β-aryl ether dimeric lignin model compound oxidation by lignin peroxidase of Phanerochaete chrysosporium. Biochemistry 25:4790–4796 · DOI
  134. Miki K, Renganathan V, Mayfield MB, Gold MH (1987) Aromatic ring cleavage of a β-biphenyl ether dimer catalyzed by lignin peroxidase of Phanerochaete chrysosporium. FEBS Lett 210:199–203 · DOI
  135. Miki Y, Tanaka H, Nakamura M, Wariishi Y (2006) Isolation and characterization of a novel lignin peroxidase from the white-rot basidiomycete Trametes cervina. J Fac Agr Kyushy Univ 51:99–104
  136. Miki Y, Morales M, Ruiz-Dueñas FJ, Martínez MJ, Wariishi H, Martínez 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 · DOI
  137. Moilanen A-M, Lundell T, Vares T, Hatakka A (1996) Manganese and malonate are individual regulators for the production of lignin and manganese peroxidase isozymes and in the degradation of lignin by Phlebia radiata. Appl Microbiol Biotechnol 45:792–799 · DOI
  138. Moreira PR, Duez C, Dehareng D, Antunes A, Almeida-Vara E, Frère JM, Malcata FX, Duarte JC (2005) Molecular characterisation of a versatile peroxidase from a Bjerkandera strain. J Biotechnol 118:339–352 · DOI
  139. Morgan JA, Lu Z, Clark DS (2002) Toward the development of a biocatalytic system for oxidation of p-xylene to terephthalic acid: oxidation of 1, 4-benzenedimethanol. J Mol Catal B: Enz 18:147–154 · DOI
  140. Morgenstern I, Klopman S, Hibbett DS (2008) Molecular evolution and diversity of lignin degrading heme peroxidases in the Agaricomycetes. J Mol Evol 66:243–257 · DOI
  141. Morris DR, Hager LP (1966) Chloroperoxidase. I. Isolation and properties of the crystalline glycoprotein. J Biol Chem 241:1763–1768 · DOI
  142. Neidleman SL, Diassi PA, Junta B, Palmere RM, Pan SC (1966) The enzymatic halogenation of steroids. Tetrahedron Lett 44:5337–5342 · DOI
  143. Newcomb M, Aebisher D, Shen R, Chandrasena RE, Hollenberg PF, Coon MJ (2003) Kinetic isotope effects implicate two electrophilic oxidants in cytochrome p450-catalyzed hydroxylations. J Am Chem Soc 125:6064–6065 · DOI
  144. Nonaka D, Wariishi H, Welinder KG, Fujii H (2010) Paramagnetic 13C and 15N NMR analyses of the push and pull effects in cytochrome c peroxidase and Coprinus cinereus peroxidase variants: functional roles of highly conserved amino acids around heme. Biochemistry 49:49–57 · DOI
  145. Nuell MJ, Fang GH, Axley MJ, Kenigsberg P, Hager LP (1988) Isolation and nucleotide sequence of the chloroperoxidase gene from Caldariomyces fumago. J Bacteriol 170:1007–1011 · DOI
  146. Ogola HJ, Kamiike T, Hashimoto N, Ashida H, Ishikawa T, Shibata H, Sawa Y (2009) Molecular characterization of a novel peroxidase from the cyanobacterium Anabaena sp. strain PCC 7120. Appl Environ Microbiol 75:7509–7518 · DOI · Paper page
  147. Oliva M, Theiler G, Zamocky M, Koua D, Margis-Pinheiro M, Passardi F, Dunand C (2009) PeroxiBase: a powerful tool to collect and analyse peroxidase sequences from Viridiplantae. J Exp Bot 60:453–459 · DOI
  148. Omura T (2005) Heme-thiolate proteins. Biochem Biophys Res Commun 338:404–409 · DOI
  149. Omura T (2010) Structural diversity of cytochrome P450 enzyme systems. J Biotechnol 147:297–306 · DOI
  150. Ortiz de Montellano P (2005) Cytochrome P450 - structure, mechanism and biochemistry, 3rd edn. Kluwer Academic/Plenum Publishers, New York · DOI
  151. Ortiz de Montellano PR, de Voss JJ (2005) Substrate oxidation by cytochrome P450 enzymes. In: Ortiz De Montellano PR (ed) Cytochrome P450 - structure, mechanism and biochemistry, 3rd edn. Kluwer Academic/Plenum Publishers, New York, pp 183–245 · DOI
  152. Ortiz-Bermudez P, Srebotnik E, Hammel KE (2003) Chlorination and cleavage of lignin structures by fungal chloroperoxidases. Appl Environ Microbiol 69:5015–5018 · DOI
  153. Ortiz-Bermudez P, Hirth KC, Srebotnik E, Hammel KE (2007) Chlorination of lignin by ubiquitous fungi has a likely role in global organochlorine production. Proc Natl Acad Sci U S A 104:3895–3900 · DOI
  154. Osborne RL, Coggins MK, Terner J, Dawson JH (2007) Caldariomyces fumago chloroperoxidase catalyzes the oxidative dehalogenation of chlorophenols by a mechanism involving two one-electron steps. J Am Chem Soc 129:14838–14389 · DOI
  155. Otey CR, Landwehr M, Endelman JB, Hiraga K, Bloom JD, Arnold FH (2006) Structure-guided recombination creates an artificial family of cytochromes P450. PLoS Biol 4:e112 · DOI
  156. Park JB, Clark DS (2006) Deactivation mechanisms of chloroperoxidase during biotransformations. Biotechnol Bioeng 93:1190–1195 · DOI
  157. Partridge M, Murphy DJ (2009) Roles of a membrane-bound caleosin and putative peroxygenase in biotic and abiotic stress responses in Arabidopsis. Plant Physiol Biochem 47:796–806 · DOI
  158. Passardi F, Bakalovic N, Teixeira FK, Margis-Pinheiro M, Penel C, Dunand C (2007a) Prokaryotic origins of the non-animal peroxidase superfamily and organelle-mediated transmission to eukaryotes. Genomics 89:567–579 · DOI
  159. Passardi F, Theiler G, Zamocky M, Cosio C, Rouhier N, Teixera F, Margis-Pinheiro M, Ioannidis V, Penel C, Falquet L, Dunand C (2007b) PeroxiBase: the peroxidase database. Phytochemistry 68:1605–1611 · DOI
  160. Pecyna MJ, Ullrich R, Bittner B, Clemens A, Scheibner K, Schubert R, Hofrichter M (2009) Molecular characterization of aromatic peroxygenase from Agrocybe aegerita. Appl Microbiol Biotechnol 84:885–897 · DOI
  161. Peng L, Wollenberger U, Hofrichter M, Ullrich R, Scheibner K, Scheller FW (2009) Bioelectrocatalytic properties of Agrocybe aegerita peroxygenase. Electrochimica Acta. doi: 10.1016/j.electacta.2009.12.065 · DOI
  162. Perez DI, Grau MM, Arends IW, Hollmann F (2009) Visible light-driven and chloroperoxidase-catalyzed oxygenation reactions. Chem Commun (Camb):6848-6850 · DOI
  163. Pérez-Boada M, Ruiz-Dueñas FJ, Pogni R, Basosi R, Choinowski T, Martínez MJ, Piontek K, Martínez AT (2005) Versatile peroxidase oxidation of high redox potential aromatic compounds: site-directed mutagenesis, spectroscopic and crystallographic investigation of three long-range electron transfer pathways. J Mol Biol 354:385–402 · DOI
  164. Petersen JF, Kadziola A, Larsen S (1994) Three-dimensional structure of a recombinant peroxidase from Coprinus cinereus at 2.6 A resolution. FEBS Lett 339:291–296 · DOI
  165. Petrides PE, Nauseef WM (2000) The peroxidase multigene family of enzymes: Biochemical basis and clinical applications 1st edn. Springer-Verlag, Berlin Heidelberg · DOI
  166. Piontek K, Glumoff T, Winterhalter K (1993) Low pH crystal structure of glycosylated lignin peroxidase from Phanerochaete chrysosporium at 2.5 A resolution. FEBS Lett 315:119–124 · DOI
  167. Piontek K, Smith AT, Blodig W (2001) Lignin peroxidase structure and function. Biochem Soc Trans 29:111–116 · DOI
  168. Piontek K, Ullrich R, Liers C, Diederichs K, Plattner D, Hofrichter M (2010) Crystallization of a 45 kDa peroxygenase/peroxidase from the mushroom Agrocybe aegerita and structure determination by SAD utilizing only the haem iron. Acta Crystallogr Sect F Struct Biol Cryst Commun 66: doi: 10.1107/S1744309110013515 · DOI
  169. Poulos TL (1993) Peroxidases. Curr Opin Biotechnol 4:484–489 · DOI
  170. Poulos TL, Freer ST, Alden RA, Xuong NH, Edwards SL, Hamlin RC, Kraut J (1978) Crystallographic determination of the heme orientation and location of the cyanide binding site in yeast cytochrome c peroxidase. J Biol Chem 253:3730–3735 · DOI
  171. Poulos TL, Edwards SL, Wariishi H, Gold MH (1993) Crystallographic refinement of lignin peroxidase at 2 A. J Biol Chem 268:4429–4440 · DOI
  172. Prieto MA, Perez-Aranda A, Garcia JL (1993) Characterization of an Escherichia coli aromatic hydroxylase with a broad substrate range. J Bacteriol 175:2162–2167 · DOI
  173. Pühse M, Szweda RT, Ma Y, Jeworrek C, Winter R, Zorn H (2009) Marasmius scorodonius extracellular dimeric peroxidase—exploring its temperature and pressure stability. Biochim Biophys Acta 1794:1091–1098 · DOI
  174. Que L Jr, Tolman WB (2008) Biologically inspired oxidation catalysis. Nature 455:333–340 · DOI
  175. Ramakrishnan K, Oppenhuizen ME, Saunders S, Fisher J (1983) Stereoselectivity of chloroperoxidase-dependent halogenation. Biochemistry 22:3271–3277 · DOI
  176. Reynolds DR, Faull JL (2001) Proposals to conserve the name Caldariomyces against Leptoxyphium and the name C. fumago with a conserved type (Ascomycota, mitosporic Euascomycetes). Taxon 50:1183–1184 · DOI
  177. Ruiz-Dueñas FJ, Martínez MJ, Martínez AT (1999) Molecular characterization of a novel peroxidase isolated from the ligninolytic fungus Pleurotus eryngii. Mol Microbiol 31:223–235 · DOI
  178. Ruiz-Dueñas FJ, Morales M, Mate MJ, Romero A, Martínez MJ, Smith AT, Martínez AT (2008) Site-directed mutagenesis of the catalytic tryptophan environment in Pleurotus eryngii versatile peroxidase. Biochemistry 47:1685–1695 · DOI
  179. Ruiz-Dueñas FJ, Morales M, Garcia E, Miki Y, Martínez MJ, Martínez AT (2009) Substrate oxidation sites in versatile peroxidase and other basidiomycete peroxidases. J Exp Bot 60:441–452 · DOI
  180. Sakurai T, Kataoka K (2007) Basic and applied features of multicopper oxidases, CueO, bilirubin oxidase, and laccase. Chem Rec 7:220–229 · DOI
  181. Sanfilippo C, Nicolosi G (2002) Catalytic behaviour of chloroperoxidase from Caldariomyces fumago in the oxidation of cyclic conjugated dienes. Tetrahedron Asymmetr 13:1889–1892 · DOI
  182. Sanfilippo C, D'Antona N, Nicolosi G (2004) Chloroperoxidase from Caldariomyces fumago is active in the presence of an ionic liquid as co-solvent. Biotechnol Lett 26:1815–1819 · DOI
  183. 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 · DOI
  184. Sato T, Hara S, Matsui T, Sazaki G, Saijo S, Ganbe T, Tanaka N, Sugano Y, Shoda M (2004) A unique dye-decolorizing peroxidase, DyP, from Thanatephorus cucumeris Dec 1: heterologous expression, crystallization and preliminary X-ray analysis. Acta Crystallogr D Biol Crystallogr 60:149–152 · DOI
  185. Savitsky PA, Gazaryan IG, Tishkov VI, Lagrimini LM, Ruzgas T, Gorton L (1999) Oxidation of indole-3-acetic acid by dioxygen catalysed by plant peroxidases: specificity for the enzyme structure. Biochem J 340(Pt3):579–583 · DOI
  186. Scheibner M, Hulsdau B, Zelena K, Nimtz M, de Boer L, Berger RG, Zorn H (2008) Novel peroxidases of Marasmius scorodonius degrade beta-carotene. Appl Microbiol Biotechnol 77:1241–1250 · DOI
  187. Schmid RD, Urlacher V (2007) Modern biooxidation enzymes, reactions and applications, 1st edn. Wiley-VCH, Weinheim · DOI
  188. Schoemaker HE, Lundell T, Hatakka A, Piontek K (1994) The oxidation of veratryl alcohol, dimeric lignin models and lignin by lignin peroxidase: the redox cycle revisioned. FEMS Microbiol Rev 13:321–332 · DOI
  189. Schomburg D, Schomburg I (2006) Class 1 oxidoreductases X. Springer handbook of enzymes, 2nd edn., vol. 25. Springer-Verlag, Berlin, Heidelberg
  190. Seelbach K, van Deurzen MP, van Rantwijk F, Sheldon RA, Kragl U (1997) Improvement of the total turnover number and space-time yield for chloroperoxidase catalyzed oxidation. Biotechnol Bioeng 55:283–288 · DOI
  191. Shaw PD, Hager LP (1959) Biological chlorination. III. beta-Ketoadipate chlorinase: a soluble enzyme system. J Biol Chem 234:2565–2569 · DOI
  192. Shimokawa T, Shoda M, Sugano Y (2009) Purification and characterization of two DyP isozymes from Thanatephorus cucumeris Dec 1 specifically expressed in an air-membrane surface bioreactor. J Biosci Bioeng 107:113–115 · DOI
  193. Singer R (1949) The Agaricales in modern taxonomy. Lilloa 22:1–832, published in 1951
  194. 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 U S A 106:16084–16089 · DOI
  195. Sturm A, Schierhorn A, Lindenstrauss U, Lilie H, Bruser T (2006) YcdB from Escherichia coli reveals a novel class of Tat-dependently translocated hemoproteins. J Biol Chem 281:13972–13978 · DOI
  196. Sugano Y (2009) DyP-type peroxidases comprise a novel heme peroxidase family. Cell Mol Life Sci 66:1387–1403 · DOI
  197. Sugano Y, Sasaki K, Shoda M (1999) cDNA cloning and genetic analysis of a novel decolorizing enzyme, peroxidase gene dyp from Geotrichum candidum Dec 1. J Biosci Bioeng 87:411–417 · DOI
  198. Sugano Y, Nakano R, Sasaki K, 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 · DOI
  199. Sugano Y, Muramatsu R, Ichiyanagi A, Sato T, Shoda M (2007) DyP, a unique dye-decolorizing peroxidase, represents a novel heme peroxidase family: ASP171 replaces the distal histidine of classical peroxidases. J Biol Chem 282:36652–36658 · DOI
  200. Sugano Y, Matsushima Y, Tsuchiya K, Aoki H, Hirai M, Shoda M (2009) Degradation pathway of an anthraquinone dye catalyzed by a unique peroxidase DyP from Thanatephorus cucumeris Dec 1. Biodegradation 20:433–440 · DOI · Paper page

200 of 242 shown

Cited by

Sorted by citations

Metadata

Authors
Hofrichter, M., Ullrich, R., Pecyna, M. J., Liers, C., & Lundell, T.
Venue
Applied Microbiology and Biotechnology
Publisher
Springer Science and Business Media LLC
Published
2010-05-22
Volume
87
Issue
3
Pages
871-897
ISSN
  • 0175-7598
  • 1432-0614
DOI
10.1007/s00253-010-2633-0
Cited by
527
References
0
Language
en
Licence
www.springer.com/tdm (tdm)

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review