Catalase and its mysteries

Progress in Biophysics and Molecular Biology

Volumn 140, Issue , 2018, Pages 5-12

  Sepasi Tehrani, Hessam ^a   Moosavi Movahedi, Ali Akbar ^b  

^a ISLAMIC AZAD UNIVERSITY   (Iran)

^b UNIVERSITY OF TEHRAN   (Iran)

Author keywords

Activity; Biophysical chemistry; Catalase; Kinetics; Mysteries; Structure; Thermodynamics

Indexed keywords

CATALASE; HYDROGEN PEROXIDE;

ANIMAL; CHEMISTRY; HUMAN; KINETICS; METABOLISM; MOLECULAR EVOLUTION; THERMODYNAMICS;

ANIMALS; CATALASE; EVOLUTION, MOLECULAR; HUMANS; HYDROGEN PEROXIDE; KINETICS; THERMODYNAMICS;

EID: 85046106141     PISSN: 00796107     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pbiomolbio.2018.03.001     Document Type: Review

References (139)

1. Abuchowski, A., McCoy, J.R., Palczuk, N.C., van Es, T., Davis, F.F., Effect of covalent attachment of polyethylene glycol on immunogenicity and circulating life of bovine liver catalase. J. Biol. Chem. 252 (1977), 3582–3586.
2. Aebi, H., Catalase in vitro. Methods Enzymol. 105 (1984), 121–126.
3. Aehle, W., Enzymes in Industry: Production and Applications. 2007, Wiley.
4. Ascone, I., Savino, C., Kahn, R., Fourme, R., Flexibility of the Cu,Zn superoxide dismutase structure investigated at 0.57 GPa. Acta Crystallogr. Sect. D Biol. Crystallogr. 66 (2010), 654–663.
5. Banerjee, R., Becker, D., Dickman, M., Gladyshev, V., Ragsdale, S., Redox Biochemistry. 2007, Wiley.
6. Beers, R.F. Jr., Sizer, I.W., A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase. J. Biol. Chem. 195 (1952), 133–140.
7. Bicout, D.J., Field, M.J., Gouet, P., Jouve, H.M., Simulations of electron transfer in the NADPH-bound catalase from Proteus mirabilis PR. Biochim. Biophys. Acta 1252 (1995), 172–176.
8. Bisswanger, H., Enzyme Kinetics: Principles and Methods. 2017, Wiley.
9. Breiten, B., Lockett, M.R., Sherman, W., Fujita, S., Al-Sayah, M., Lange, H., Bowers, C.M., Heroux, A., Krilov, G., Whitesides, G.M., Water networks contribute to enthalpy/entropy compensation in protein–ligand binding. J. Am. Chem. Soc. 135 (2013), 15579–15584.
10. Brezniceanu, M.L., Liu, F., Wei, C.C., Tran, S., Sachetelli, S., Zhang, S.L., Guo, D.F., Filep, J.G., Ingelfinger, J.R., Chan, J.S., Catalase overexpression attenuates angiotensinogen expression and apoptosis in diabetic mice. Kidney Int. 71 (2007), 912–923.
11. Chang, T., Poznansky, M., Semipermeable microcapsules containing catalase for enzyme replacement in acatalasaemic mice. Nature 218 (1968), 243–245.
12. Cheetham, N.W.H., Introducing Biological Energetics: How Energy and Information Control the Living World. 2011, OUP, Oxford.
13. Chelikani, P., Fita, I., Loewen, P.C., Diversity of structures and properties among catalases. Cell. Mol. Life Sci. 61 (2004), 192–208.
14. Chelikani, P., Ramana, T., Radhakrishnan, T.M., Catalase: a repertoire of unusual features. Indian J. Clin. Biochem. 20 (2005), 131–135.
15. Copeland, R.A., Evaluation of Enzyme Inhibitors in Drug Discovery: a Guide for Medicinal Chemists and Pharmacologists. 2013, John Wiley & Sons.
16. Cornish-Bowden, A., Biochemical Evolution: The Pursuit of Perfection. second ed., 2016, Garland Science.
17. Csukas, S., Costarides, A., Riley, M.V., Green, K., Hydrogen peroxide in the rabbit anterior chamber: effects on glutathione, and catalase effects on peroxide kinetics. Curr. Eye Res. 6 (1987), 1395–1402.
18. DeJong, R.J., Miller, L.M., Molina-Cruz, A., Gupta, L., Kumar, S., Barillas-Mury, C., Reactive oxygen species detoxification by catalase is a major determinant of fecundity in the mosquito Anopheles gambiae. Proc. Natl. Acad. Sci. U. S. A. 104 (2007), 2121–2126.
19. Del Rio, L.A., Ortega, M.G., Lopez, A.L., Gorge, J.L., A more sensitive modification of the catalase assay with the Clark oxygen electrode. Application to the kinetic study of the pea leaf enzyme. Anal. Biochem. 80 (1977), 409–415.
20. Domański, L., Safranow, K., Dołȩgowska, B., Różański, J., Myślak, M., Ciechanowski, K., Jakubowska, K., Dziedziejko, V., Romanowski, M., Sulikowski, T., Sieńko, J., Kamiński, M., Ostrowski, M., Domański, M., Pawlik, A., Rać M.E. and Chlubek, D. Hypoxanthine as a graft ischemia marker stimulates catalase activity in the renal vein during reperfusion in humans, Transplantation Proceedings. 38, 35–38.
21. Dunford, H.B., Peroxidases and Catalases: Biochemistry, Biophysics, Biotechnology and Physiology. 2010, Wiley.
22. Epp, O., Ladenstein, R., Wendel, A., The refined structure of the selenoenzyme glutathione peroxidase at 0.2-nm resolution. Eur. J. Biochem. 133 (1983), 51–69.
23. Escobar, L., Salvador, C., Contreras, M., Escamilla, J.E., On the application of the Clark oxygen electrode to the study of enzyme kinetics in apolar solvents: the catalase reaction. Anal. Biochem. 184 (1990), 139–144.
24. Fita, I., Rossmann, M.G., The NADPH binding site on beef liver catalase. Proc. Natl. Acad. Sci. U.S.A. 82 (1985), 1604–1608.
25. Freire, E., Do enthalpy and entropy distinguish first in class from best in class?. Drug Discov. Today 13 (2008), 869–874.
26. Gaetani, G., Kirkman, H., Mangerini, R., Ferraris, A., Importance of catalase in the disposal of hydrogen peroxide within human erythrocytes. Blood 84 (1994), 325–330.
27. Ghadermarzi, M., Moosavi-Movahedi, A.A., Determination of the kinetic parameters for the “suicide substrate” inactivation of bovine liver catalase by hydrogen peroxide. J. Enzym. Inhib. 10 (1996), 167–175.
28. Ghadermarzi, M., Moosavi-Movahedi, A.A., Influence of different types of effectors on the kinetic parameters of suicide inactivation of catalase by hydrogen peroxide. Biochim. Biophys. Acta 1431 (1999), 30–36.
29. Glorieux, C., Calderon, P.B., Catalase, a remarkable enzyme: targeting the oldest antioxidant enzyme to find a new cancer treatment approach. Biol. Chem. 398 (2017), 1095–1108.
30. Góth, L., Bigler, N.W., Catalase deficiency may complicate urate oxidase (rasburicase) therapy. Free Radic. Res. 41 (2007), 953–955.
31. Goth, L., Eaton, J.W., Hereditary catalase deficiencies and increased risk of diabetes. Lancet 356 (2000), 1820–1821.
32. Goth, L., Nagy, T., Inherited catalase deficiency: is it benign or a factor in various age related disorders?. Mutat. Res. Rev. Mutat. Res. 753 (2013), 147–154.
33. Hamada, Y., Kameyama, Y., Iizuka, T., Ishizaki, T., Nishiyama, T., Isshiki, A., Methemoglobinemia from hydrogen peroxide in a patient with acatalasemia. J. Am. Soc. Anesthesiologists 101 (2004), 247–248.
34. Hanwell, M.D., Curtis, D.E., Lonie, D.C., Vandermeersch, T., Zurek, E., Hutchison, G.R., Avogadro: an advanced semantic chemical editor, visualization, and analysis platform. J. Cheminf., 4, 2012 17–17.
35. Hara, I., Ichise, N., Kojima, K., Kondo, H., Ohgiya, S., Matsuyama, H., Yumoto, I., Relationship between the size of the bottleneck 15 A from iron in the main channel and the reactivity of catalase corresponding to the molecular size of substrates. Biochemistry 46 (2007), 11–22.
36. Heck, D.E., Vetrano, A.M., Mariano, T.M., Laskin, J.D., UVB light stimulates production of reactive oxygen species: unexpected role for catalase. J. Biol. Chem. 278 (2003), 22432–22436.
37. Hertz, P.E., Russell, P., General Biology. 2007, Thomson Learning EMEA, Limited.
38. Ho, Y.-S., Xiong, Y., Ma, W., Spector, A., Ho, D.S., Mice lacking catalase develop normally but show differential sensitivity to oxidant tissue injury. J. Biol. Chem. 279 (2004), 32804–32812.
39. Holdgate, G., Fisher, S., Ward, W., The Application of Isothermal Titration Calorimetry to Drug Discovery. 2004, John Wiley & Sons Ltd, West Sussex.
40. Hong, J., Wang, W., Huang, K., Yang, W.Y., Zhao, Y.X., Xiao, B.L., Gao, Y.F., Moosavi-Movahedi, Z., Ghourchian, H., Moosavi-Movahedi, A.A., A highly efficient nano-cluster artificial peroxidase and its direct electrochemistry on a nano complex modified glassy carbon electrode. Anal. Sci. 28 (2012), 711–716.
41. Ivancich, A., Loewen, P.C., Electron transfer in catalases and catalase-peroxidases. Roberts, G.C.K., (eds.) Encyclopedia of Biophysics, 2013, Springer Berlin Heidelberg, Berlin, Heidelberg, 611–614.
42. Izawa, S., Inoue, Y., Kimura, A., Importance of catalase in the adaptive response to hydrogen peroxide: analysis of acatalasaemic Saccharomyces cerevisiae. Biochem. J. 320:Pt 1 (1996), 61–67.
43. Jakopitsch, C., Droghetti, E., Schmuckenschlager, F., Furtmuller, P.G., Smulevich, G., Obinger, C., Role of the main access channel of catalase-peroxidase in catalysis. J. Biol. Chem. 280 (2005), 42411–42422.
44. Jakopitsch, C., Wanasinghe, A., Jantschko, W., Furtmuller, P.G., Obinger, C., Kinetics of interconversion of ferrous enzymes, compound II and compound III, of wild-type synechocystis catalase-peroxidase and Y249F: proposal for the catalatic mechanism. J. Biol. Chem. 280 (2005), 9037–9042.
45. Jemec, A., Drobne, D., Tisler, T., Sepcic, K., Biochemical biomarkers in environmental studies–lessons learnt from enzymes catalase, glutathione S-transferase and cholinesterase in two crustacean species. Environ. Sci. Pollut. Res. Int. 17 (2010), 571–581.
46. 2 access to the heme cavity of catalase KatE of Escherichia coli. Arch. Biochem. Biophys. 526 (2012), 54–59.
47. Jones, M.N., Finn, A., Moosavi-Movahedi, A.A., Waller, B.J., The activation of Aspergillus Niger catalase by sodium n-dodecyl-sulphate. Biochim. Biophys. Acta 913 (1987), 395–398.
48. Kalpakcioglu, B., Senel, K., The interrelation of glutathione reductase, catalase, glutathione peroxidase, superoxide dismutase, and glucose-6-phosphate in the pathogenesis of rheumatoid arthritis. Clin. Rheumatol. 27 (2008), 141–145.
49. Khan, M.V., Zaman, M., Chandel, T.I., Siddiqui, M.K., Ajmal, M.R., Abdelhameed, A.S., Khan, R.H., Cationic surfactant mediated fibrillogenesis in bovine liver catalase: a biophysical approach. J. Biomol. Struct. Dyn., 2017, 1–15.
50. Kim, S., Thiessen, P.A., Bolton, E.E., Chen, J., Fu, G., Gindulyte, A., Han, L., He, J., He, S., Shoemaker, B.A., Wang, J., Yu, B., Zhang, J., Bryant, S.H., PubChem substance and compound databases. Nucleic Acids Res. 44 (2016), D1202–D1213.
51. Kirkman, H.N., Gaetani, G.F., Mammalian catalase: a venerable enzyme with new mysteries. Trends Biochem. Sci. 32 (2007), 44–50.
52. Kitani, K., Kanai, S., Carrillo, M.C., Ivy, G.O., (-)Deprenyl increases the life span as well as activities of superoxide dismutase and catalase but not of glutathione peroxidase in selective brain regions in Fischer rats. Ann. N. Y. Acad. Sci. 717 (1994), 60–71.
53. Klinger, W., Karge, E., Kretzschmar, M., Rost, M., Schulze, H.P., Dargel, R., Reinemann, C., Rein, H., Luminol-and lucigenin-amplified chemiluminescence with rat liver microsomes. Kinetics and influence of ascorbic acid, glutathione, dimethylsulfoxide, N-t-butyl-a-phenyl-nitrone, copper-ions and a copper complex, catalase, superoxide dismutase, hexobarbital and aniline. Exp. Toxicol. Pathol. 48 (1996), 447–460.
54. Ko, T.P., Day, J., Malkin, A.J., McPherson, A., Structure of orthorhombic crystals of beef liver catalase. Acta Crystallogr. Sect. D Biol. Crystallogr. 55 (1999), 1383–1394.
55. Koechling, U.M., Amit, Z., Negrete, J.C., Family history of alcoholism and the mediation of alcohol intake by catalase: further evidence for catalase as a marker of the propensity to ingest alcohol. Alcohol Clin. Exp. Res. 19 (1995), 1096–1104.
56. Krumova, K., Cosa, G., Overview of Reactive Oxygen Species. 2016.
57. Krych-Madej, J., Gebicka, L., Interactions of nitrite with catalase: enzyme activity and reaction kinetics studies. J. Inorg. Biochem. 171 (2017), 10–17.
58. Krych, J., Gebicka, L., Catalase is inhibited by flavonoids. Int. J. Biol. Macromol. 58 (2013), 148–153.
59. Krych, J., Gebicki, J.L., Gebicka, L., Flavonoid-induced conversion of catalase to its inactive form–Compound II. Free Radic. Res. 48 (2014), 1334–1341.
60. Ladbury, J.E., Klebe, G., Freire, E., Adding calorimetric data to decision making in lead discovery: a hot tip. Nat. Rev. Drug Discov. 9 (2010), 23–27.
61. Laskowski, M., Sumner, J.B., Crystalline catalase from beef erythrocytes. Science, 94, 1941, 615.
62. Lazarow, P.B., De Duve, C., A fatty acyl-CoA oxidizing system in rat liver peroxisomes; enhancement by clofibrate, a hypolipidemic drug. Proc. Natl. Acad. Sci. Unit. States Am. 73 (1976), 2043–2046.
63. Lei, X.G., Zhu, J.-H., Cheng, W.-H., Bao, Y., Ho, Y.-S., Reddi, A.R., Holmgren, A., Arnér, E.S.J., Paradoxical roles of antioxidant enzymes: basic mechanisms and health implications. Physiol. Rev. 96 (2016), 307–364.
64. Liu, Y., Eisenberg, D., 3D domain swapping: as domains continue to swap. Protein Sci. : Publ. Protein Soc. 11 (2002), 1285–1299.
65. Loew, O., A new enzyme of general occurrence in organisms. Science 11 (1900), 701–702.
66. López-Lázaro, M., Dual role of hydrogen peroxide in cancer: possible relevance to cancer chemoprevention and therapy. Canc. Lett. 252 (2007), 1–8.
67. Machuqueiro, M., Victor, B., Switala, J., Villanueva, J., Rovira, C., Fita, I., Loewen, P.C., The catalase activity of catalase-peroxidases is modulated by changes in the pKa of the distal histidine. Biochemistry 56 (2017), 2271–2281.
68. Martinelli, L.K.B., Rotta, M., Villela, A.D., Rodrigues-Junior, V.S., Abbadi, B.L., Trindade, R.V., Petersen, G.O., Danesi, G.M., Nery, L.R., Pauli, I., Campos, M.M., Bonan, C.D., de Souza, O.N., Basso, L.A., Santos, D.S., Functional, thermodynamics, structural and biological studies of in silico-identified inhibitors of Mycobacterium tuberculosis enoyl-ACP(CoA) reductase enzyme. Sci. Rep., 7, 2017, 46696.
69. Mascarenhas, N.M., Gosavi, S., Understanding protein domain-swapping using structure-based models of protein folding. Prog. Biophys. Mol. Biol. 128 (2017), 113–120.
70. Michiels, C., Raes, M., Toussaint, O., Remacle, J., Importance of Se-glutathione peroxidase, catalase, and Cu/Zn-SOD for cell survival against oxidative stress. Free Radic. Biol. Med. 17 (1994), 235–248.
71. Mofidi Najjar, F., Ghadari, R., Yousefi, R., Safari, N., Sheikhhasani, V., Sheibani, N., Moosavi-Movahedi, A.A., Studies to reveal the nature of interactions between catalase and curcumin using computational methods and optical techniques. Int. J. Biol. Macromol. 95 (2017), 550–556.
72. Mofidi Najjar, F., Taghavi, F., Ghadari, R., Sheibani, N., Moosavi-Movahedi, A.A., Destructive effect of non-enzymatic glycation on catalase and remediation via curcumin. Arch. Biochem. Biophys. 630 (2017), 81–90.
73. Moosavi-Movahedi, A.A., Ghobadi, S., Thermochemical analysis of Aspergillus Niger catalase and sodium n-dodecyl sulphate interaction. Thermochim. Acta 189 (1991), 201–207.
74. Moosavi-Movahedi, A.A., Jones, M., Pilcher, G., Thermodynamics of the interaction of sodium n-dodecyl sulphate with Aspergillus Niger catalase in low ionic strength aqueous solutions. Int. J. Biol. Macromol. 10 (1988), 75–78.
75. Moosavi-Movahedi, A.A., Wilkinson, A., Jones, M., Characterization of Aspergillus Niger catalase. Int. J. Biol. Macromol. 9 (1987), 327–332.
76. Moosavi-Movahedi, A.A., Jones, M.M., Pilcher, G., Thermodynamics of the interaction of sodium-n-dodecyl sulphate with Aspergillus Niger catalase in high ionic strength aqueous solutions. Int. J. Biol. Macromol. 11 (1989), 26–28.
77. 2 : kinetic equations for peroxidatic oxidation reaction of guaiacol and determination of the kinetic parameters. Ital. J. Biochem. 48 (1999), 9–17.
78. Moosavi-Movahedi, A.A., Pilcher, G., Jones, M., Thermodynamics of the interaction between n-dodecyltrimethylammonium bromide and catalases. Thermochim. Acta 146 (1989), 215–223.
79. Moser, C.C., Chobot, S.E., Page, C.C., Dutton, P.L., Distance metrics for heme protein electron tunneling. Biochim. Biophys. Acta 1777 (2008), 1032–1037.
80. Murakami, S., Fukushima, K., Ishikawa, A., Yamazaki, I., Visualization of surface structure of catalase crystals by metal decoration. J. Electron. Microsc.(Tokyo) 33 (1984), 401–404.
81. Murthy, M.R., Reid, T.J. 3rd, Sicignano, A., Tanaka, N., Rossmann, M.G., Structure of beef liver catalase. J. Mol. Biol. 152 (1981), 465–499.
82. Nicholls, P., Fita, I., Loewen, P.C., Enzymology and structure of catalases. Adv. Inorg. Chem. 51 (2000), 51–106.
83. O'Neill, S., Inactivation of immobilized catalase by hydrogen peroxide in continuous reactors. Biotechnol. Bioeng. 14 (1972), 201–205.
84. Orsi, N.M., Leese, H.J., Protection against reactive oxygen species during mouse preimplantation embryo development: role of EDTA, oxygen tension, catalase, superoxide dismutase and pyruvate. Mol. Reprod. Dev. 59 (2001), 44–53.
85. Ortiz de Montellano, P.R., Kerr, D.E., Inactivation of catalase by phenylhydrazine. Formation of a stable aryl-iron heme complex. J. Biol. Chem. 258 (1983), 10558–10563.
86. Özmen, B., Özmen, D., Erkin, E., Güner, I.n., Habif, S., Bayındır, O., Lens superoxide dismutase and catalase activities in diabetic cataract. Clin. Biochem. 35 (2002), 69–72.
87. Perozzo, R., Folkers, G., Scapozza, L., Thermodynamics of protein–ligand interactions: history, presence, and future aspects. J. Recept. Signal Transduct. Res. 24 (2004), 1–52.
88. Pichorner, H., Jessner, G., Ebermann, R., tBOOH acts as a suicide substrate for catalase. Arch. Biochem. Biophys. 300 (1993), 258–264.
89. Porollo, A., Meller, J., Versatile annotation and publication quality visualization of protein complexes using POLYVIEW-3D. BMC Bioinf., 8, 2007, 316.
90. Porter, D., Bright, H., Ethanenitronate is a peroxide-dependent suicide substrate for catalase. J. Biol. Chem. 262 (1987), 9608–9614.
91. Potapovich, M.V., Eremin, A.N., Metelitsa, D.I., Kinetics of catalase inactivation induced by ultrasonic cavitation. Prikl. Biokhim. Mikrobiol. 39 (2003), 160–166.
92. Regelsberger, G., Jakopitsch, C., Furtmuller, P.G., Rueker, F., Switala, J., Loewen, P.C., Obinger, C., The role of distal tryptophan in the bifunctional activity of catalase-peroxidases. Biochem. Soc. Trans. 29 (2001), 99–105.
93. Reid, T.J. 3rd, Murthy, M.R., Sicignano, A., Tanaka, N., Musick, W.D., Rossmann, M.G., Structure and heme environment of beef liver catalase at 2.5 A resolution. Proc. Natl. Acad. Sci. U. S. A. 78 (1981), 4767–4771.
94. Rhee, S.G., Yang, K.S., Kang, S.W., Woo, H.A., Chang, T.S., Controlled elimination of intracellular H(2)O(2): regulation of peroxiredoxin, catalase, and glutathione peroxidase via post-translational modification. Antioxidants Redox Signal. 7 (2005), 619–626.
95. Rorth, M., Jensen, P.K., Determination of catalase activity by means of the Clark oxygen electrode. Biochim. Biophys. Acta 139 (1967), 171–173.
96. Ross, P.D., Subramanian, S., Thermodynamics of protein association reactions: forces contributing to stability. Biochemistry 20 (1981), 3096–3102.
97. Rousseau, F., Schymkowitz, J., Itzhaki, L.S., Implications of 3D Domain Swapping for Protein Folding, Misfolding and Function, Protein Dimerization and Oligomerization in Biology. 2012, Springer, 137–152.
98. Rozwarski, D.A., Grant, G.A., Barton, D.H., Jacobs, W.R., Sacchettini, J.C., Modification of the NADH of the isoniazid target (InhA) from Mycobacterium tuberculosis. Science 279 (1998), 98–102.
99. Schaefer, J., Lee, G., Arrhenius activation energy of damage to catalase during spray-drying. Int. J. Pharm. 489 (2015), 124–130.
100. Schallreuter, K.U., Elwary, S., Hydrogen peroxide regulates the cholinergic signal in a concentration dependent manner. Life Sci. 80 (2007), 2221–2226.
101. Schriner, S.E., Linford, N.J., Extension of mouse lifespan by overexpression of catalase. Age 28 (2006), 209–218.
102. Schriner, S.E., Linford, N.J., Martin, G.M., Treuting, P., Ogburn, C.E., Emond, M., Coskun, P.E., Ladiges, W., Wolf, N., Van Remmen, H., Extension of murine life span by overexpression of catalase targeted to mitochondria. Science 308 (2005), 1909–1911.
103. Sepasi Tehrani, H., Moosavi-Movahedi, A.A., Ghourchian, H., Ahmad, F., Kiany, A., Atri, M.S., Ariaeenejad, S., Kavousi, K., Saboury, A.A., Effect of compatible and noncompatible osmolytes on the enzymatic activity and thermal stability of bovine liver catalase. J. Biomol. Struct. Dyn. 31 (2013), 1440–1454.
104. Sepasi Tehrani, H., Moosavi-Movahedi, A.A., Ghourchian, H., Correlation between biological activity and electron transferring of bovine liver catalase: osmolytes effects. Electrochim. Acta 113 (2013), 591–602.
105. Shen, Y., Li, D., Tian, P., Shen, K., Zhu, J., Feng, M., Wan, C., Yang, T., Chen, L., Wen, F., The catalase C-262T gene polymorphism and cancer risk: a systematic review and meta-analysis. Medicine (Baltim.), 94, 2015, e679.
106. Shi, Y., Lo, C.S., Chenier, I., Maachi, H., Filep, J.G., Ingelfinger, J.R., Zhang, S.L., Chan, J.S., Overexpression of catalase prevents hypertension and tubulointerstitial fibrosis and normalization of renal angiotensin-converting enzyme-2 expression in Akita mice. Am. J. Physiol. Ren. Physiol. 304 (2013), F1335–F1346.
107. Siddiqui, K.S., Ertan, H., Charlton, T., Poljak, A., Daud Khaled, A.K., Yang, X., Marshall, G., Cavicchioli, R., Versatile peroxidase degradation of humic substances: use of isothermal titration calorimetry to assess kinetics, and applications to industrial wastes. J. Biotechnol. 178 (2014), 1–11.
108. Singh, R., Wiseman, B., Deemagarn, T., Donald, L.J., Duckworth, H.W., Carpena, X., Fita, I., Loewen, P.C., Catalase-peroxidases (KatG) exhibit NADH oxidase activity. J. Biol. Chem. 279 (2004), 43098–43106.
109. Smulevich, G., Jakopitsch, C., Droghetti, E., Obinger, C., Probing the structure and bifunctionality of catalase-peroxidase (KatG). J. Inorg. Biochem. 100 (2006), 568–585.
110. Starr, C., Taggart, R., Biology: the Unity and Diversity of Life. 2005, Cengage Learning.
111. Stone, J.R., Yang, S., Hydrogen peroxide: a signaling messenger. Antioxidants Redox Signal. 8 (2006), 243–270.
112. Suarez, J., Ranguelova, K., Jarzecki, A.A., Manzerova, J., Krymov, V., Zhao, X., Yu, S., Metlitsky, L., Gerfen, G.J., Magliozzo, R.S., An oxyferrous heme/protein-based radical intermediate is catalytically competent in the catalase reaction of mycobacterium tuberculosis catalase-peroxidase (KatG). J. Biol. Chem. 284 (2009), 7017–7029.
113. Sumner, J.B., Dounce, A.L., Crystalline catalase. Science 85 (1937), 366–367.
114. Sumner, J.B., Gralen, N., The molecular weight of crystalline catalase. Science, 87, 1938, 284.
115. Sykes, A., Mauk, G., Heme-fe Proteins. 2000, Elsevier Science.
116. Takahara, S., Hamilton, H.B., Neel, J.V., Kobara, T.Y., Ogura, Y., Nishimura, E.T., Hypocatalasemia: a new genetic Carrier state. J. Clin. Invest. 39 (1960), 610–619.
117. Takahara, S., Miyamoto, H., Three cases of progressive oral gangrene due to lack of catalase in the blood. Jpn. J. Otol. 51 (1948), 163–168.
118. Thompson, V.S., Schaller, K.D., Apel, W.A., Purification and characterization of a novel thermo-alkali-stable catalase from Thermus brockianus. Biotechnol. Prog. 19 (2003), 1292–1299.
119. Tovmasyan, A., Maia, C.G., Weitner, T., Carballal, S., Sampaio, R.S., Lieb, D., Ghazaryan, R., Ivanovic-Burmazovic, I., Ferrer-Sueta, G., Radi, R., A comprehensive evaluation of catalase-like activity of different classes of redox-active therapeutics. Free Radic. Biol. Med. 86 (2015), 308–321.
120. Unwin, P.N., Beef liver catalase structure: interpretation of electron micrographs. J. Mol. Biol. 98 (1975), 235–242.
121. Vainshtein, B.K., Melik-Adamyan, W.R., Barynin, V.V., Vagin, A.A., Grebenko, A.I., Three-dimensional structure of the enzyme catalase. Nature 293 (1981), 411–412.
122. Valderrama, B., Ayala, M., Vazquez-Duhalt, R., Suicide inactivation of peroxidases and the challenge of engineering more robust enzymes. Chem. Biol. 9 (2002), 555–565.
123. Vasudevan, P.T., Thakur, D.S., Soluble and immobilized catalase. Effect of pressure and inhibition on kinetics and deactivation. Appl. Biochem. Biotechnol. 49 (1994), 173–189.
124. Vidossich, P., Loewen, P.C., Carpena, X., Fiorin, G., Fita, I., Rovira, C., Binding of the antitubercular pro-drug isoniazid in the heme access channel of catalase-peroxidase (KatG). A combined structural and metadynamics investigation. J. Phys. Chem. B 118 (2014), 2924–2931.
125. Vives-Bauza, C., Starkov, A., Garcia-Arumi, E., Measurements of the antioxidant enzyme activities of superoxide dismutase, catalase, and glutathione peroxidase. Meth. Cell Biol. 80 (2007), 379–393.
126. Vlasits, J., Bellei, M., Jakopitsch, C., De Rienzo, F., Furtmuller, P.G., Zamocky, M., Sola, M., Battistuzzi, G., Obinger, C., Disruption of the H-bond network in the main access channel of catalase-peroxidase modulates enthalpy and entropy of Fe(III) reduction. J. Inorg. Biochem. 104 (2010), 648–656.
127. Wang, R., Zhang, L., Wang, R., Dou, H., Li, H., Wang, Y., Pu, J., Wang, R., Spectroscopic study on the interaction of catalase with bifendate and analogs. Spectrochim. Acta Mol. Biomol. Spectrosc. 102 (2013), 88–98.
128. Watson, J.D., Type 2 diabetes as a redox disease. Lancet 383 (2014), 841–843.
129. Wu, S., Li, Q., Du, M., Li, S.Y., Ren, J., Cardiac-specific overexpression of catalase prolongs lifespan and attenuates ageing-induced cardiomyocyte contractile dysfunction and protein damage. Clin. Exp. Pharmacol. Physiol. 34 (2007), 81–87.
130. Yang, B., Hao, F., Li, J., Chen, D., Liu, R., Binding of chrysoidine to catalase: spectroscopy, isothermal titration calorimetry and molecular docking studies. J. Photochem. Photobiol., B 128 (2013), 35–42.
131. Yang, H., Roberts, L.J., Shi, M.J., Zhou, L.C., Ballard, B.R., Richardson, A., Guo, Z.M., Retardation of atherosclerosis by overexpression of catalase or both Cu/Zn-superoxide dismutase and catalase in mice lacking apolipoprotein E. Circ. Res. 95 (2004), 1075–1081.
132. Yang, T., Poovaiah, B.W., Hydrogen peroxide homeostasis: activation of plant catalase by calcium/calmodulin. Proc. Natl. Acad. Sci. U. S. A. 99 (2002), 4097–4102.
133. Yasmineh, W.G., Kaur, T.P., Blazar, B.R., Theologides, A., Serum catalase as marker of graft-vs-host disease in allogeneic bone marrow transplant recipients: pilot study. Clin. Chem. 41 (1995), 1574–1580.
134. Yekta, R., Dehghan, G., Rashtbari, S., Sheibani, N., Moosavi-Movahedi, A.A., Activation of catalase by pioglitazone: multiple spectroscopic methods combined with molecular docking studies. J. Mol. Recogn. 30 (2017), 2648–2658.
135. Zamocky, M., Gasselhuber, B., Furtmuller, P.G., Obinger, C., Turning points in the evolution of peroxidase-catalase superfamily: molecular phylogeny of hybrid heme peroxidases. Cell. Mol. Life Sci. 71 (2014), 4681–4696.
136. Zamocky, M., Herzog, C., Nykyri, L.M., Koller, F., Site-directed mutagenesis of the lower parts of the major substrate channel of yeast catalase A leads to highly increased peroxidatic activity. FEBS Lett. 367 (1995), 241–245.
137. Zámocký M., Koller, F., Understanding the structure and function of catalases: clues from molecular evolution and in vitro mutagenesis. Prog. Biophys. Mol. Biol. 72 (1999), 19–66.
138. Zhang, R., Piao, M.J., Oh, M.C., Park, J.E., Shilnikova, K., Moon, Y.J., Kim, D.H., Jung, U., Kim, I.G., Hyun, J.W., Protective effect of an isoflavone, tectorigenin, against oxidative stress-induced cell death via catalase activation. J. Cancer Prev. 21 (2016), 257–263.
139. Zhao, X., Hersleth, H.P., Zhu, J., Andersson, K.K., Magliozzo, R.S., Access channel residues Ser315 and Asp137 in Mycobacterium tuberculosis catalase-peroxidase (KatG) control peroxidatic activation of the pro-drug isoniazid. Chem. Commun. 49 (2013), 11650–11652.