Ferric haem forms of Mycobacterium tuberculosis catalase-peroxidase probed by EPR spectroscopy: Their stability and interplay with pH

Biochimie

Volumn 94, Issue 6, 2012, Pages 1274-1280

  Svistunenko, Dimitri A ^a   Worrall, Jonathan A R ^a   Chugh, Snehpriya B ^a   Haigh, Sarah C ^a   Ghiladi, Reza A ^b   Nicholls, Peter ^a  

^a UNIVERSITY OF ESSEX   (United Kingdom)

^b NORTH CAROLINA STATE UNIVERSITY   (United States)

Author keywords

Catalase peroxidase; EPR; High spin; HS; Mycobacterium tuberculosis

Indexed keywords

BUFFER; FERRIC ION; HEME; KATG PROTEIN; METHANOL;

ARTICLE; ELECTRON SPIN RESONANCE; ENZYME ACTIVE SITE; EQUILIBRIUM CONSTANT; FREEZING; LOW TEMPERATURE PROCEDURES; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; OXIDATION; PH; PROTEIN STABILITY; STORAGE; TIME;

BACTERIAL PROTEINS; CATALASE; COLD TEMPERATURE; ELECTRON SPIN RESONANCE SPECTROSCOPY; ENZYME STABILITY; FERRIC COMPOUNDS; HEME; HYDROGEN-ION CONCENTRATION; MODELS, MOLECULAR; MYCOBACTERIUM TUBERCULOSIS; PEROXIDASES;

MYCOBACTERIUM TUBERCULOSIS;

EID: 84860444501     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2012.02.021     Document Type: Article

References (29)

1. K.G. Welinder Bacterial catalase-peroxidases are gene duplicated members of the plant peroxidase superfamily Biochim. Biophys. Acta 1080 1991 215 220
2. Y. Yamada, T. Fujiwara, T. Sato, N. Igarashi, and N. Tanaka The 2.0 A crystal structure of catalase-peroxidase from Haloarcula marismortui Nat. Struct. Biol. 9 2002 691 695 (Pubitemid 34977303)
3. M. Zámocký, G. Regelsberger, C. Jakopitsch, and C. Obinger The molecular peculiarities of catalase-peroxidases FEBS Lett. 492 2001 177 182 (Pubitemid 32217824)
4. T. Bertrand, N.A. Eady, J.N. Jones, Jesmin, J.M. Nagy, B. Jamart-Gregoire, E.L. Raven, and K.A. Brown Crystal structure of Mycobacterium tuberculosis catalase-peroxidase J. Biol. Chem. 279 2004 38991 38999 (Pubitemid 39296060)
5. Y. Zhang, B. Heym, B. Allen, D. Young, and S. Cole The catalase-peroxidase gene and isoniazid resistance of Mycobacterium tuberculosis Nature 358 1992 591 593
6. E.H. Robitzek, and I.J. Selikoff Hydrazine derivatives of isonicotinic acid (rimifon marsilid) in the treatment of active progressive caseous-pneumonic tuberculosis; a preliminary report Am. Rev. Tuberc. 65 1952 402 428
7. J.M. Musser, V. Kapur, D.L. Williams, B.N. Kreiswirth, D. van Soolingen, and J.D. van Embden Characterization of the catalase-peroxidase gene (katG) and inhA locus in isoniazid-resistant and -susceptible strains of Mycobacterium tuberculosis by automated DNA sequencing: restricted array of mutations associated with drug resistance J. Infect. Dis. 173 1996 196 202
8. D.A. Rouse, J.A. DeVito, Z.M. Li, H. Byer, and S.L. Morris Site-directed mutagenesis of the katG gene of Mycobacterium tuberculosis: effects on catalase-peroxidase activities and isoniazid resistance Mol. Microbiol. 22 1996 583 592 (Pubitemid 26373841)
9. R.S. Magliozzo, and J.A. Marcinkeviciene Evidence for isoniazid oxidation by oxyferrous mycobacterial catalase-peroxidase J. Am. Chem. Soc. 118 1996 11303 11304 (Pubitemid 26399760)
10. B. Lei, C.J. Wei, and S.C. Tu Action mechanism of antitubercular isoniazid. Activation by Mycobacterium tuberculosis KatG, isolation, and characterization of InhA inhibitor J. Biol. Chem. 275 2000 2520 2526 (Pubitemid 30082015)
11. R.A. Ghiladi, K.F. Medzihradszky, F.M. Rusnak, and P.R. Ortiz de Montellano Correlation between isoniazid resistance and superoxide reactivity in Mycobacterium tuberculosis KatG J. Am. Chem. Soc. 127 2005 13428 13442 (Pubitemid 41377636)
12. J. Suarez, K. Ranguelova, J.P. Schelvis, and R.S. Magliozzo Antibiotic resistance in Mycobacterium tuberculosis: peroxidase intermediate bypass causes poor isoniazid activation by the S315G mutant of M. tuberculosis catalase-peroxidase (KatG) J. Biol. Chem. 284 2009 16146 16155
13. H. Ando, T. Kitao, T. Miyoshi-Akiyama, S. Kato, T. Mori, and T. Kirikae Downregulation of katG expression is associated with isoniazid resistance in Mycobacterium tuberculosis Mol. Microbiol. 79 2011 1615 1628
14. th position in M. tuberculosis catalase-peroxidase enzyme and isoniazid susceptibility: an in silico analysis J. Mol. Model. 17 2011 869 877
15. S. Chouchane, S. Girotto, S. Kapetanaki, J.P. Schelvis, S. Yu, and R.S. Magliozzo Analysis of heme structural heterogeneity in Mycobacterium tuberculosis catalase-peroxidase (KatG) J. Biol. Chem. 278 2003 8154 8162 (Pubitemid 36800557)
16. R. Singh, J. Switala, P.C. Loewen, and A. Ivancich Two [Fe(IV)=O Trp*] intermediates in M. tuberculosis catalase-peroxidase discriminated by multifrequency (9-285 GHz) EPR spectroscopy: reactivity toward isoniazid J. Am. Chem. Soc. 129 2007 15954 15963
17. J. Peisach, W.E. Blumberg, S. Ogawa, E.A. Rachmilewitz, and R. Oltzik The effect of protein conformation on the heme symmetry in high spin ferric heme proteins as studied by electron paramagnetic resonance J. Biol. Chem. 246 1971 3342 3355
18. M.K. Thompson, S. Franzen, R.A. Ghiladi, B.J. Reeder, and D.A. Svistunenko Compound ES of dehaloperoxidase decays via two alternative pathways depending on the conformation of the distal histidine J. Am. Chem. Soc. 132 2010 17501 17510
19. J.A. Weil, J.R. Bolton, and J.E. Wertz Electron Paramagnetic Resonance: Elementary Theory and Practical Applications 1994 John Wiley & Sons, Inc. New York
20. D.A. Svistunenko Reaction of haem containing proteins and enzymes with hydroperoxides: the radical view Biochim. Biophys. Acta 1707 2005 127 155 (Pubitemid 40253588)
21. D.A. Svistunenko, N. Davies, D. Brealey, M. Singer, and C.E. Cooper Mitochondrial dysfunction in patients with severe sepsis: an EPR interrogation of individual respiratory chain components Biochim. Biophys. Acta 1757 2006 262 272
22. C.A. Appleby, W.E. Blumberg, J. Peisach, B.A. Wittenberg, and J.B. Wittenberg Leghemoglobin. An electron paramagnetic resonance and optical spectral study of the free protein and its complexes with nicotinate and acetate J. Biol. Chem. 251 1976 6090 6096
23. D.L. Williams-Smith, R.C. Bray, M.J. Barber, A.D. Tsopanakis, and S.P. Vincent Changes in apparent pH on freezing aqueous buffer solutions and their relevance to biochemical electron-paramagnetic-resonance spectroscopy Biochem. J. 167 1977 593 600 (Pubitemid 8240975)
24. D.A. Svistunenko, R.P. Patel, and M.T. Wilson An EPR investigation of human methaemoglobin oxidation by hydrogen peroxide: methods to quantify all paramagnetic species observed in the reaction Free Radical Res. 24 1996 269 280 (Pubitemid 26144650)
25. J. Peisach, W.E. Blumberg, B.A. Wittenberg, and J.B. Wittenberg The electron structure of protoheme proteins. III. Configuration of the heme and its ligands J. Biol. Chem. 243 1968 1871 1880
26. J. Peisach, W.E. Blumberg, B.A. Wittenberg, J.B. Wittenberg, and L. Kampa Hemoglobin A: an electron paramagnetic resonance study of the effects of interchain contacts on the heme symmetry of high-spin and low-spin derivatives of ferric alpha chains Proc. Natl. Acad. Sci. U.S.A. 63 1969 934 939
27. D.A. Svistunenko, M.A. Sharpe, P. Nicholls, C. Blenkinsop, N.A. Davies, J. Dunne, M.T. Wilson, and C.E. Cooper The pH dependence of naturally occurring low-spin forms of methaemoglobin and metmyoglobin: an EPR study Biochem. J. 351 2000 595 605
28. X.B. Zhao, H. Yu, S.W. Yu, F. Wang, J.C. Sacchettini, and R.S. Magliozzo Hydrogen peroxide-mediated isoniazid activation catalyzed by Mycobacterium tuberculosis catalase-peroxidase (KatG) and its S315T mutant Biochemistry 45 2006 4131 4140
29. X. Carpena, B. Wiseman, T. Deemagarn, B. Herguedas, A. Ivancich, R. Singh, P.C. Loewen, and I. Fita Roles for Arg426 and Trp111 in the modulation of NADH oxidase activity of the catalase-peroxidase KatG from Burkholderia pseudomallei inferred from pH-induced structural changes Biochemistry 45 2006 5171 5179