Structural evidence for the order of preference of inorganic substrates in mammalian heme peroxidases: Crystal structure of the complex of lactoperoxidase with four inorganic substrates, SCN -, I -, Br - and Cl -

International Journal of Biochemistry and Molecular Biology

Volumn 2, Issue 4, 2011, Pages 328-339

  Singh, Amit K ^a   Pandey, Nisha ^a   Sinha, Mau ^a   Kaur, Punit ^a   Sharma, Sujata ^a   Singh, Tej P ^a  

^a ALL INDIA INSTITUTE OF MEDICAL SCIENCES   (India)

Author keywords

Antimicrobial activity; Complex; Crystal structure; Halide ions; Heme; Oxidation; Peroxidase

Indexed keywords

HEME; INORGANIC COMPOUND; IRON; LACTOPEROXIDASE; PSEUDOHALIDE; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; BINDING SITE; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME SUBSTRATE; HYDROGEN BOND; STEREOCHEMISTRY; STRUCTURE ANALYSIS;

MAMMALIA;

EID: 84863395364     PISSN: None     EISSN: 21524114     Source Type: Journal    
DOI: None     Document Type: Article

References (33)

1. Zhang H, Dunford HB. Hammett pδ correlation for reactions of lactoperoxidase compound II with phenols. Can J Chem 1993; 71: 1990-1994.
2. Monzani E, Gatti AL, Profumo A, Casella L and Gullotti M. Oxidation of phenolic compounds by lactoperoxidase. Evidence for the presence of a low-potential compound II during catalytic turnover. Biochemistry 1997; 36: 1918-1926.
3. Metodiewa D, Reszka K and Dunford HB. Oxidation of the substituted catechols dihydroxy-phenylalanine methyl ester and trihydroxy-phenylalanine by lactoperoxidase and its compounds. Arch Biochem Biophys 1989; 274: 601-608.
4. Metodiewa D, Reszka K and Dunford HB. Evidence for a peroxidatic oxidation of norepineph-rine, a catecholamine, by lactoperoxidase. Bio-chem Biophys Res Commun 1989; 160: 1183-1188.
5. Ferrari RP, Laurenti E, Casella L and Poli S. Oxidation of catechols and catecholamines by horseradish-peroxidase and lactoperoxidase: ESR spin stabilization approach combined with optical methods. Spectrochim Acta 1993; 49: 1261-1267.
6. Doerge DR, Decker CJ. Inhibition of peroxidase-catalyzed reactions by arylamines: mechanism for the anti-thyroid action of sulfamethazine. Chem Res Toxicol 1994; 7: 164-169.
7. Oakley GG, Devanaboyina U, Robertson LW and Gupta RC. Oxidative DNA damage induced by activation of polychlorinated biphenyls (PCBs): implications for PCB-induced oxidative stress in breast cancer. Chem Res Toxicol 1996; 9: 1285-1292.
8. Sipe HJ, Jr Jordan SJ, Hanna PM and Mason RP. The metabolism of 17 beta-estradiol by lactoperoxidase: a possible source of oxidative stress in breast cancer. Carcinogenesis 1994, 15: 2637-2643.
9. Cavalieri EL, Stack DE, Devanesan PD, Todorovic R, Dwivedy I, Higginbotham S, Johansson SL, Patil KD, Gross ML, Gooden JK, Rama-nathan R, Cerny RL and Rogan EG. Molecular origin of cancer: catechol estrogen-3,4-quinones as endogenous tumor initiators. Proc Natl Acad Sci USA 1997; 94: 10937-10942.
10. Ghibaudi EM, Laurenti E, Beltramo P and Ferrari RP. Can estrogenic radicals, generated by lactoperoxidase, be involved in the molecular mechanism of breast carcinogenesis? Redox Rep 2000; 5: 229-235.
11. RamaKrishna NV, Li KM, Rogan EG, Cavalieri EL, George M, Cerny RL and Gross ML. Adducts of 6-methylbenzo[a]pyrene and 6-fluorobenzo [a]pyrene formed by electrochemical oxidation in the presence of deoxyribonucleosides. Chem Res Toxicol 1993; 6: 837-845.
12. Zeng J, Fenna RE. X-ray crystal structure of canine myeloperoxidase at 3Å resolution. J Mol Biol 1992; 226: 185-207.
13. Davey CA, Fenna RE. 2.3Å resolution X-ray crystal structure of the bisubstrate analogue inhibitor salicylhydroxamic acid bound to human myeloperoxidase: a model for a prereaction complex with hydrogen peroxide. Biochemistry 1996, 35: 10967-10973.
14. Fiedler TJ, Davey CA and Fenna RE. X-ray crystal structure and characterization of halide-binding sites of human myeloperoxidase at 1.8Å resolution. J Biol Chem 2000; 275: 11964-11971.
15. Blair-Johnson M, Fiedler T and Fenna R. Human myeloperoxidase: structure of a cyanide complex and its interaction with bromide and thio-cyanate substrates at 1.9Å resolution. Biochemistry 2001; 40: 13990-13997.
16. Singh AK, Singh N, Sharma S, Singh SB, Kaur, P, Bhushan A, Srinivasan A and Singh TP. Crystal structure of lactoperoxidase at 2.4Å resolution. J Mol Biol 2008; 376: 1060-1075.
17. Singh AK, Singh N, Sharma S, Shin K, Takase M, Kaur P, Srinivasan A and Singh TP. Inhibition of lactoperoxidase by its own catalytic product: crystal structure of the hypothiocyanate-inhibited bovine lactoperoxidase at 2.3Å resolution. Biophys J 2009; 96: 646-654.
18. Sheikh IA, Singh AK, Singh N, Sinha M, Singh SB, Bhushan A, Kaur P, Srinivasan A, Sharma S and Singh TP. Structural evidence of substrate specificity in mammalian peroxidases: structure of the thiocyanate complex with lactoperoxi-dase and its interactions at 2.4Å resolution. J Biol Chem 2009; 284: 14849-14856.
19. Singh AK, Singh N, Sinha M, Bhushan A, Kaur P, Srinivasan A, Sharma S and Singh TP. Binding modes of aromatic ligands to mammalian heme peroxidases with associated functional implications: crystal structures of lactoperoxi-dase complexes with acetylsalicylic acid, salicyl-hydroxamic acid, and benzylhydroxamic acid. J Biol Chem 2009; 284: 20311-20318.
20. Singh AK, Kumar RP, Pandey N, Singh N, Sinha M, Bhushan A, Kaur P, Sharma S and Singh TP. Mode of binding of the tuberculosis prodrug isoniazid to heme peroxidases: binding studies and crystal structure of bovine lactoperoxidase with isoniazid at 2.7Å resolution. J Biol Chem 2010; 285: 1569-1576.
21. Singh AK, Singh N, Tiwari A, Sinha M, Kushwaha GS, Kaur P, Srinivasan, A, Sharma S and Singh TP. First structural evidence for the mode of diffusion of aromatic ligands and ligand-induced closure of the hydrophobic channel in heme peroxidases. J Biol Inorg Chem 2010; 15: 1099-1107.
22. Ferrari RP, Ghibaudi EM, Traversa S, Laurenti E, De Gioia L and Salmona M. Spectroscopic and binding studies on the interaction of inorganic anions with lactoperoxidase. J Inorg Biochem 1997; 68: 17-26.
23. Harrison JE, Schultz J. Studies on the chlorinating activity of myeloperoxidase. J Biol Chem 1976; 251: 1371-1374.
24. van Dalen CJ, Kettle AJ. Substrates and products of eosinophil peroxidase. Biochem J 2001; 358: 233-239.
25. Kimura S, Kotani T, McBride OW, Umeki K, Hirai K, Nakayama T and Ohtaki S. Human thyroid peroxidase: complete cDNA and protein sequence, chromosome mapping, and identification of two alternately spliced mRNAs. Proc Natl Acad Sci USA 1987; 84: 5555-5559.
26. Shindler JS, Bardsley WG. Steady-state kinetics of lactoperoxidase with ABTS as chromogen. Biochem Biophys Res Commun 1975; 67: 1307-1312.
27. Otwinowski Z, Minor W. Processing of X-ray Diffraction Data Collected in Oscillation Mode. Methods in Enzymology 1997; 276: 307-326.
28. Brunger AT, Adams PD, Clore GM, DeLano WL, Gros P, Grosse-Kunstleve RW, Jiang JS, Kuszewski J, Nilges M, Pannu NS, Read RJ, Rice LM, Simonson T and Warren GL. Crystallography & NMR system: A new software suite for macromolecular structure determination. Acta Crystallogr 1998; D54: 905-921.
29. Jones TA, Zou JY, Cowan SW and Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr 1991; A47: 110-119.
30. Laskowski RA, Macarthur M, Moss D and Thornton J. PROCHECK: a program to check stereo chemical quality of protein structures. J Appl Crystallogr 1993; 26: 283-290.
31. Ramachandran GN, Sasisekaran V. Conformation of polypeptides and proteins. Adv Protein Chem 1968; 23: 283-438.
32. Davis IW, Leaver-Fay A, Chen VB, Block JN, Kapral GJ, Wang X, Murray LW, Arendall WB 3rd, Snoeyink J, Richardson JS and Richardson DC. MolProbity: all-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res 2007; 35: W375-383.
33. DeLano WL. The PyMol molecular Graphics System, DeLano Scientific, San Carlos CA. 2002; http://www.pymol.org.