Exploring the catalase activity of unspecific peroxygenases and the mechanism of peroxide-dependent heme destruction

Journal of Molecular Catalysis B: Enzymatic

Volumn 134, Issue , 2016, Pages 238-246

  Karich, Alexander ^a   Scheibner, Katrin ^b   Ullrich, René ^a   Hofrichter, Martin ^a  

^a International Graduate School Zittau   (Germany)

^b BRANDENBURG UNIVERSITY OF TECHNOLOGY   (Germany)

Author keywords

Catalase; Heme; Inactivation; Peroxygenase

Indexed keywords

PIGMENTS;

APPARENT KINETIC PARAMETERS; CATALASE; COPRINOPSIS CINEREA; ENZYME INACTIVATION; HEME; HYDROXYL RADICAL FORMATION; INACTIVATION; PEROXYGENASE;

PORPHYRINS;

BENZOIC ACID; BILIVERDIN; CATALASE; HEME; HYDROXYL RADICAL; OXYGEN; OXYGENASE; PEROXIDE; UNCLASSIFIED DRUG; UNSPECIFIC PEROXYGENASE;

AGROCYBE AEGERITA; ARTICLE; BASIDIOMYCETES; BLEACHING; COPRINOPSIS CINEREA; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME INACTIVATION; ENZYME MECHANISM; KINETIC PARAMETERS; MARASMIUS; MARASMIUS ROTULA; NONHUMAN; PH; REACTION ANALYSIS; SIGNAL TRANSDUCTION;

EID: 85000714924     PISSN: 13811177     EISSN: 18733158     Source Type: Journal    
DOI: 10.1016/j.molcatb.2016.10.014     Document Type: Article

References (72)

1. [1] Karich, A., Kluge, M., Ullrich, R., Hofrichter, M., AMB Express, 3, 2013, 5.
2. [2] Aranda, E., Kinne, M., Kluge, M., Ullrich, R., Hofrichter, M., Appl. Microbiol. Biotechnol. 82 (2009), 1057–1066.
3. [3] Ullrich, R., Dolge, C., Kluge, M., Hofrichter, M., FEBS Lett. 582 (2008), 4100–4106.
4. [4] Kinne, M., Poraj-Kobielska, M., Ralph, S.A., Ullrich, R., Hofrichter, M., Hammel, K.E., J. Biol. Chem. 284 (2009), 29343–29349.
5. [5] Ullrich, R., Nüske, J., Scheibner, K., Spantzel, J., Hofrichter, M., Appl. Environ. Microbiol. 70 (2004), 4575–4581.
6. [6] Aranda, E., Ullrich, R., Hofrichter, M., Biodegradation 21 (2010), 267–281.
7. [7] Barková, K., Kinne, M., Ullrich, R., Hennig, L., Fuchs, A., Hofrichter, M., Tetrahedron 67 (2011), 4874–4878.
8. [8] Peter, S., Kinne, M., Wang, X., Ullrich, R., Kayser, G., Groves, J., Hofrichter, M., FEBS J. 278 (2011), 3667–3675.
9. [9] Poraj-Kobielska, M., Kinne, M., Ullrich, R., Scheibner, K., Kayser, G., Hammel, K.E., Hofrichter, M., Biochem. Pharmacol. 82 (2011), 789–796.
10. [10] Kluge, M., Ullrich, R., Scheibner, K., Hofrichter, M., Green Chem. 14 (2012), 440–446.
11. [11] Hofrichter, M., Kellner, H., Pecyna, M.J., Ullrich, R., Adv. Exp. Med. Biol. 851 (2015), 341–368.
12. [12] Churakova, E., Kluge, M., Ullrich, R., Arends, I., Hofrichter, M., Hollmann, F., Angew. Chem. Int. Ed. 50 (2011), 10716–10719.
13. [13] Valderrama, B., Ayala, M., Vazquez-Duhalt, R., Chem. Biol. 9 (2002), 555–565.
14. [14] Vlasits, J., Jakopitsch, C., Bernroitner, M., Zamocky, M., Furtmüller, P.G., Obinger, C., Arch. Biochem. Biophys. 500 (2010), 74–81.
15. [15] Shevelkova, A.N., Ryabov, A.D., IUBMB Life 39 (1996), 665–670.
16. [16] Karuzina, I.I., Archakov, A.I., Free Radic. Biol. Med. 17 (1994), 557–567.
17. [17] Arnao, M.B., Acosta, M., del Rio, J.A., García-Cánovas, F., Biochim. Biophys. Acta (BBA) 1038 (1990), 85–89.
18. [18] Hiner, A.N., Rodríguez-López, J.N., Arnao, M.B., Lloyd Raven, E., García-Cánovas, F., Acosta, M., Biochem. J. 348 (2000), 321–328.
19. [19] Chang, H.C., Holland, R.D., Bumpus, J.A., Churchwell, M.I., Doerge, D.R., Chem. Biol. Interact. 123 (1999), 197–217.
20. [20] Vidal-Limón, A., Águila, S., Ayala, M., Batista, C.V., Vazquez-Duhalt, R., J. Inorg. Biochem. 122 (2013), 18–26.
21. [21] Wariishi, H., Gold, M.H., J. Biol. Chem. 265 (1990), 2070–2077.
22. [22] Hiner, A.N.P., Martínez, J.I., Arnao, M.B., Acosta, M., Turner, D.D., Lloyd Raven, E., Rodríguez-López, J.N., Eur. J. Biochem. 268 (2001), 3091–3098.
23. [23] Blodig, W., Doyle, W.A., Smith, A.T., Winterhalter, K., Choinowski, T., Piontek, K., Biochemistry (Mosc.) 37 (1998), 8832–8838.
24. [24] Pogni, R., Baratto, M.C., Giansanti, S., Teutloff, C., Verdin, J., Valderrama, B., Lendzian, F., Lubitz, W., Vazquez-Duhalt, R., Basosi, R., Biochemistry (Mosc.) 44 (2005), 4267–4274.
25. [25] Ayala, M., Batista, C.V., Vazquez-Duhalt, R., JBIC J. Biol. Inorg. Chem. 16 (2010), 63–68.
26. [26] Wang, X., Peter, S., Ullrich, R., Hofrichter, M., Groves, J.T., Angew. Chem. Int. Ed. 52 (2013), 9238–9241.
27. [27] Wang, X., Peter, S., Kinne, M., Hofrichter, M., Groves, J.T., J. Am. Chem. Soc. 134 (2012), 12897–12900.
28. [28] Wang, X., Ullrich, R., Hofrichter, M., Groves, J.T., Proc. Natl. Acad. Sci. 112 (2015), 3686–3691.
29. [29] Kühnel, K., Derat, E., Terner, J., Shaik, S., Schlichting, I., Proc. Natl. Acad. Sci. 104 (2007), 99–104.
30. [30] Palcic, M.M., Rutter, R., Araiso, T., Hager, L.P., Dunford, H.B., Biochem. Biophys. Res. Commun. 94 (1980), 1123–1127.
31. [31] Nakajima, R., Yamazaki, I., Griffin, B.W., Biochem. Biophys. Res. Commun. 128 (1985), 1–6.
32. [32] Valderrama, B., Deactivation of hemeperoxidases by hydrogen peroxide: focus on compound III. Torres, E., Ayala, M., (eds.) Biocatalysis Based on Heme Peroxidases: Peroxidases as Potential Industrial Biocatalysts, 2010, Springer Berlin Heidelberg, Berlin, Heidelberg, 291–314.
33. [33] Liu, Y., Moënne-Loccoz, P., Loehr, T.M., de Montellano, P.R.O., J. Biol. Chem. 272 (1997), 6909–6917.
34. [34] Tenhunen, R., Marver, H.S., Schmid, R., J. Biol. Chem. 244 (1969), 6388–6394.
35. [35] Ortiz de Montellano, P.R., Acc. Chem. Res. 31 (1998), 543–549.
36. [36] Lai, W., Chen, H., Matsui, T., Omori, K., Unno, M., Ikeda-Saito, M., Shaik, S., J. Am. Chem. Soc. 132 (2010), 12960–12970.
37. [37] Kikuchi, G., Yoshida, T., Noguchi, M., Biochem. Biophys. Res. Commun. 338 (2005), 558–567.
38. [38] Gheidi, M., Safari, N., Bahrami, H., Zahedi, M., J. Inorg. Biochem. 101 (2007), 385–395.
39. [39] Gröbe, G., Ullrich, R., Pecyna, M., Kapturska, D., Friedrich, S., Hofrichter, M., Scheibner, K., AMB Express, 1, 2011, 31.
40. [40] Babot, E.D., del Río, J.C., Kalum, L., Martínez, A.T., Gutiérrez, A., Biotechnol. Bioeng. 110 (2013), 2323–2332.
41. [41] Morrison, M., Horie, S., Anal. Biochem. 12 (1965), 77–82.
42. [42] Sagone, A.L., Decker, M.A., Wells, R.M., Democko, C., Biochim. Biophys. Acta (BBA) 628 (1980), 90–97.
43. [43] Das, D.K., George, A., Liu, X., Rao, P.S., Biochem. Biophys. Res. Commun. 165 (1989), 1004–1009.
44. [44] Hofrichter, M., Ullrich, R., Pecyna, M., Liers, C., Lundell, T., Appl. Microbiol. Biotechnol. 87 (2010), 871–897.
45. [45] Piontek, K., Ullrich, R., Liers, C., Diedrichs, K., Plattner, A.D., Hofrichter, M., Acta Crystallogr. Sect. F 66 (2010), 693–698.
46. [46] Piontek, K., Strittmatter, E., Dimitrova, B., Zámocky, M., Kiebist, J., Ullrich, R., Hofrichter, M., Scheibner, K., Dietmar, P.A., J. Biol. Chem., 2016 (Submitted for publication).
47. [47] Walling, C., Acc. Chem. Res. 8 (1975), 125–131.
48. [48] Manoj, K.M., Hager, L.P., Biochim. Biophys. Acta (BBA) 1547 (2001), 408–417.
49. [49] Thomas, J.A., Morris, D.R., Hager, L.P., J. Biol. Chem. 245 (1970), 3129–3134.
50. [50] Zaks, A., Dodds, D.R., J. Am. Chem. Soc. 117 (1995), 10419–10424.
51. [51] Manoj, K.M., Hager, L.P., Biochemistry (Mosc.) 47 (2008), 2997–3003.
52. [52] Sundaramoorthy, M., Terner, J., Poulos, T.L., Structure 3 (1995), 1367–1378.
53. [53] Piontek, K., Strittmatter, E., Ullrich, R., Gröbe, G., Pecyna, M.J., Kluge, M., Scheibner, K., Hofrichter, M., Plattner, D.A., J. Biol. Chem. 288 (2013), 34767–34776.
54. [54] Park, J.-B., Clark, D.S., Biotechnol. Bioeng. 93 (2006), 1190–1195.
55. [55] Denisov, I.G., Sligar, S.G., Nat. Chem. 7 (2015), 687–688.
56. [56] Ni, Y., Fernández-Fueyo, E., Baraibar, A.G., Ullrich, R., Hofrichter, M., Yanase, H., Alcalde, M., van Berkel, W.J.H., Hollmann, F., Angew. Chem. Int. Ed. 55 (2016), 798–801.
57. [57] Ullrich, R., Nuske, J., Scheibner, K., Spantzel, J., Hofrichter, M., Appl. Environ. Microbiol. 70 (2004), 4575–4581.
58. [58] Unno, M., Matsui, T., Ikeda-Saito, M., Nat. Prod. Rep. 24 (2007), 553–570.
59. [59] Matsui, T., Iwasaki, M., Sugiyama, R., Unno, M., Ikeda-Saito, M., Inorg. Chem. 49 (2010), 3602–3609.
60. [60] Baek, H.K., Van Wart, H.E., Biochemistry (Mosc.) 28 (1989), 5714–5719.
61. [61] Ullrich, R., Hofrichter, M., FEBS Lett. 579 (2005), 6247–6250.
62. [62] Halliwell H, B.K., Ingelman-Sundberg, M., Free Radical Biol. Med. 10 (1990), 439–441.
63. [63] Kluge, M., Ullrich, R., Dolge, C., Scheibner, K., Hofrichter, M., Appl. Microbiol. Biotechnol. 81 (2009), 1071–1076.
64. [64] Kasperek, G.J., Bruice, T.C., J. Am. Chem. Soc. 94 (1972), 198–202.
65. [65] Díaz-Díaz, G., Blanco-López, M.C., Lobo-Castañón, M.J., Miranda-Ordieres, A.J., Tuñón-Blanco, P., J. Mol. Catal. B: Enzym. 66 (2010), 332–336.
66. [66] Haber, F., Weiss, J., Proc. R. Soc. Lond. A 147 (1934), 332–351.
67. [67] Cohen, G., Heikkila, R.E., MacNamee, W.t.t.a.o.D., J. Biol. Chem. 249 (1974), 2447–2452.
68. [68] Chen, S.-x., Schopfer, P., Eur. J. Biochem. 260 (1999), 726–735.
69. [69] Adediran, S.A., Arch. Biochem. Biophys. 327 (1996), 279–284.
70. [70] Ullrich, R., Hofrichter, M., Cell. Mol. Life Sci. 64 (2007), 271–293.
71. [71] Vidossich, P., Magistrato, A., Biomolecules, 4, 2014, 616.
72. [72] Alfonso-Prieto, M., Biarnés, X., Vidossich, P., Rovira, C., J. Am. Chem. Soc. 131 (2009), 11751–11761.