Properties of catalase-peroxidase lacking its C-terminal domain

Biochemical and Biophysical Research Communications

Volumn 320, Issue 3, 2004, Pages 833-839

  Baker, Ruletha D ^a   Cook, Carma O ^a   Goodwin, Douglas C ^a  

^a AUBURN UNIVERSITY   (United States)

Author keywords

Catalase peroxidase; Deletion mutagenesis; Heme; KatG; Lignin peroxidase; Manganese peroxidase

Indexed keywords

CATALASE; CYANIDE; HISTIDINE; PEROXIDASE;

ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; ELECTRON SPIN RESONANCE; ENZYME ANALYSIS; ENZYME STRUCTURE; MEASUREMENT; PRIORITY JOURNAL; SPECTROSCOPY;

AMINO ACID SUBSTITUTION; BACTERIAL PROTEINS; CARBON; ENZYME ACTIVATION; ENZYME STABILITY; ESCHERICHIA COLI; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; PEROXIDASES; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN STRUCTURE, TERTIARY; RECOMBINANT PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 3042760502     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.06.026     Document Type: Article

References (35)

1. Loewen P.C. Bacterial catalases. Scandalios J.G. Oxidative Stress and the Molecular Biology of Antioxidant Defenses. 1997;273-308 Cold Spring Harbor Laboratory Press, Plainview, NY
2. Zhang Y., Heym B., Allen B., Young D., Cole S. The catalase-peroxidase gene and isoniazid resistance of Mycobacterium tuberculosis. Nature. 358:1992;591-593
3. Rattan A., Kalia A., Ahmad N. Multidrug-resistant Mycobacterium tuberculosis: molecular perspectives. Emerg. Infect. Dis. 4:1998;195-209
4. Garcia E., Nedialkov Y.A., Elliott J., Motin V.L., Brubaker R.R. Molecular characterization of KatY (antigen 5), a thermoregulated chromosomally encoded catalase-peroxidase of Yersinia pestis. J. Bacteriol. 181:1999;3114-3122
5. Brunder W., Schmidt H., Karch H. KatP, a novel catalase-peroxidase encoded by the large plasmid of enterohaemorrhagic Escherichia coli O157:H7. Microbiology. 142:1996;3305-3315
6. Mehigh R.J., Brubaker R.R. Major stable peptides of Yersinia pestis synthesized during the low-calcium response. Infect. Immun. 61:1993;13-22
7. Bandyopadhyay P., Steinman H.M. Catalase-peroxidases of Legionella pneumophila: cloning of the katA gene and studies of KatA function. J. Bacteriol. 182:2000;6679-6686
8. Bandyopadhyay P., Byrne B., Chan Y., Swanson M.S., Steinman H.M. Legionella pneumophila catalase-peroxidases are required for proper trafficking and growth in primary macrophages. Infect. Immun. 71:2003;4526-4535
9. Varnado C.L., Hertwig K.M., Thomas R., Roberts J.K., Goodwin D.C. Properties of a novel periplasmic catalase-peroxidase from Escherichia coli O157:H7. Arch. Biochem. Biophys. 421:2004;166-174
10. Jakopitsch C., Auer M., Regelsberger G., Jantschko W., Furtmuller P.G., Ruker F., Obinger C. Distal site aspartate is essential in the catalase activity of catalase-peroxidases. Biochemistry. 42:2003;5292-5300
11. Yamada Y., Fujiwara T., Sato T., Igarashi N., Tanaka N. The 2.0. Å crystal structure of catalase-peroxidase from Haloarcula marismortui Nat. Struct. Biol. 9:2002;691-695
12. Carpena X., Loprasert S., Mongkolsuk S., Switala J., Loewen P.C., Fita I. Catalase-peroxidase KatG of Burkholderia pseudomallei at 1.7. Å resolution J. Mol. Biol. 327:2003;475-489
13. Zamocky M., Regelsberger G., Jakopitsch C., Obinger C. The molecular peculiarities of catalase-peroxidases. FEBS Lett. 492:2001;177-182
14. Welinder K.G. Bacterial catalase-peroxidases are gene duplicated members of the plant peroxidase superfamily. Biochim. Biophys. Acta. 1080:1991;215-220
15. Sambrook J., Maniatis T., Fritsch E.F. Molecular Cloning: A Laboratory Manual. 1989;Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
16. Li Y., Goodwin D.C. Vital roles of an interhelical insertion in catalase-peroxidase bifunctionality. Biochem. Biophys. Res. Commun. 318:2004;970-976
17. Claiborne A., Fridovich I. Purification of the o-dianisidine peroxidase from Escherichia coli B. Physicochemical characterization and analysis of its dual catalatic and peroxidatic activities. J. Biol. Chem. 254:1979;4245-4252
18. Hillar A., Peters B., Pauls R., Loboda A., Zhang H., Mauk A.G., Loewen P.C. Modulation of the activities of catalase-peroxidase HPI of Escherichia coli by site-directed mutagenesis. Biochemistry. 39:2000;5868-5875
19. Chouchane S., Girotto S., Kapetanaki S., Schelvis J.P., Yu S., Magliozzo R.S. Analysis of heme structural heterogeneity in Mycobacterium tuberculosis catalase-peroxidase (KatG). J. Biol. Chem. 278:2003;8154-8162
20. Kengen S.W., Bikker F.J., Hagen W.R., de Vos W.M., van der Oost J. Characterization of a catalase-peroxidase from the hyperthermophilic archaeon Archaeoglobus fulgidus. Extremophiles. 5:2001;323-332
21. Gadsby P.M.A., Thomson A.J. Assignment of the axial ligands of ferric ion in low-spin hemoproteins by near-infrared magnetic circular dichroism and electron paramagnetic resonance spectroscopy. J. Am. Chem. Soc. 112:1990;5003-5011
22. Palmer G. Electron paramagnetic resonance of hemoproteins. Dolphin D. The Porphyrins: Physical Chemistry, Part B. 1979;313-350 Academic Press, New York
23. Sutherland G.R., Zapanta L.S., Tien M., Aust S.D. Role of calcium in maintaining the heme environment of manganese peroxidase. Biochemistry. 36:1997;3654-3662
24. Nie G., Aust S.D. Effect of calcium on the reversible thermal inactivation of lignin peroxidase. Arch. Biochem. Biophys. 337:1997;225-231
25. Banci L., Bartalesi I., Ciofi-Baffoni S., Tien M. Unfolding and pH studies on manganese peroxidase: role of heme and calcium on secondary structure stability. Biopolymers. 72:2003;38-47
26. 2+ and heme. J. Biol. Chem. 265:1990;13335-13343
27. Whitwam R.E., Gazarian I.G., Tien M. Expression of fungal Mn peroxidase in E. coli and refolding to yield active enzyme. Biochem. Biophys. Res. Commun. 216:1995;1013-1017
28. Nie G., Reading N.S., Aust S.D. Expression of the lignin peroxidase H2 gene from Phanerochaete chrysosporium in Escherichia coli. Biochem. Biophys. Res. Commun. 249:1998;146-150
29. Poulos T.L., Edwards S.L., Wariishi H., Gold M.H. Crystallographic refinement of lignin peroxidase at 2. Å J. Biol. Chem. 268:1993;4429-4440
30. Sundaramoorthy M., Kishi K., Gold M.H., Poulos T.L. The crystal structure of manganese peroxidase from Phanerochaete chrysosporium at 2.06. Å resolution J. Biol. Chem. 269:1994;32759-32767
31. Sutherland G.R., Aust S.D. Thermodynamics of binding of the distal calcium to manganese peroxidase. Biochemistry. 36:1997;8567-8573
32. Nie G., Aust S.D. Spectral changes of lignin peroxidase during reversible inactivation. Biochemistry. 36:1997;5113-5119
33. Dunford H.B., Stillman J.S. On the function and mechanism of action of peroxidases. Coord. Chem. Rev. 19:1976;187-251
34. Erman J.E., Vitello L.B., Miller M.A., Shaw A., Brown K.A., Kraut J. Histidine 52 is a critical residue for rapid formation of cytochrome c peroxidase compound I. Biochemistry. 32:1993;9798-9806
35. Regelsberger G., Jakopitsch C., Ruker F., Krois D., Peschek G.A., Obinger C. Effect of distal cavity mutations on the formation of compound I in catalase-peroxidases. J. Biol. Chem. 275:2000;22854-22861