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Human myeloperoxidase: structure of a cyanide complex and its interaction with bromide and thiocyanate substrates at 1.9 A resolution.

Blair-Johnson M, Fiedler T, Fenna R
Biochemistry 40 13990-7 (2001)
Related entries: 1d7w, 1dnu, 1dnw, 1mhl

Cited: 60 times
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Abstract

The 1.9 A X-ray crystal structure of human myeloperoxidase complexed with cyanide (R = 0.175, R(free) = 0.215) indicates that cyanide binds to the heme iron with a bent Fe-C-N angle of approximately 157 degrees, and binding is accompanied by movement of the iron atom by 0.2 A into the porphyrin plane. The bent orientation of the cyanide allows the formation of three hydrogen bonds between its nitrogen atom and the distal histidine as well as two water molecules in the distal cavity. The 1.85 A X-ray crystal structure of an inhibitory complex with thiocyanate (R = 0.178, R(free) = 0.210) indicates replacement of chloride at a proximal helix halide binding site in addition to binding in the distal cavity in an orientation parallel with the heme. The thiocyanate replaces two water molecules in the distal cavity and is hydrogen bonded to Gln 91. The 1.9 A structures of the complexes formed by bromide (R = 0.215, R(free) = 0.270) and thiocyanate (R = 0.198, R(free) = 0.224) with the cyanide complex of myeloperoxidase show how the presence of bound cyanide alters the binding site for bromide in the distal heme cavity, while having little effect on thiocyanate binding. These results support a model for a single common binding site for halides and thiocyanate as substrates or as inhibitors near the delta-meso carbon of the porphyrin ring in myeloperoxidase.

Reviews - 1d5l mentioned but not cited (1)

  1. Myeloperoxidase: a target for new drug development? Malle E, Furtmüller PG, Sattler W, Obinger C. Br. J. Pharmacol. 152 838-854 (2007)


Reviews citing this publication (12)

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  15. The vinyl-sulfonium bond in human myeloperoxidase: impact on compound I formation and reduction by halides and thiocyanate. Zederbauer M, Furtmüller PG, Ganster B, Moguilevsky N, Obinger C. Biochem. Biophys. Res. Commun. 356 450-456 (2007)
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  17. Myeloperoxidase-catalyzed taurine chlorination: initial versus equilibrium rate. Ramos DR, Victoria García M, Canle L M, Arturo Santaballa J, Furtmüller PG, Obinger C. Arch. Biochem. Biophys. 466 221-233 (2007)
  18. Ciona intestinalis peroxinectin is a novel component of the peroxidase-cyclooxygenase gene superfamily upregulated by LPS. Vizzini A, Parrinello D, Sanfratello MA, Mangano V, Parrinello N, Cammarata M. Dev. Comp. Immunol. 41 59-67 (2013)
  19. Geometries and electronic structures of cyanide adducts of the non-heme iron active site of superoxide reductases: vibrational and ENDOR studies. Clay MD, Yang TC, Jenney FE, Kung IY, Cosper CA, Krishnan R, Kurtz DM, Adams MW, Hoffman BM, Johnson MK. Biochemistry 45 427-438 (2006)
  20. Myeloperoxidase-catalyzed chlorination: the quest for the active species. Ramos DR, García MV, Canle L M, Santaballa JA, Furtmüller PG, Obinger C. J. Inorg. Biochem. 102 1300-1311 (2008)
  21. CO binding and ligand discrimination in human myeloperoxidase. Murphy EJ, Maréchal A, Segal AW, Rich PR. Biochemistry 49 2150-2158 (2010)
  22. How covalent heme to protein bonds influence the formation and reactivity of redox intermediates of a bacterial peroxidase. Auer M, Nicolussi A, Schütz G, Furtmüller PG, Obinger C. J. Biol. Chem. 289 31480-31491 (2014)
  23. 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. Singh AK, Pandey N, Sinha M, Kaur P, Sharma S, Singh TP. Int J Biochem Mol Biol 2 328-339 (2011)
  24. Histidine 386 and its role in cyclooxygenase and peroxidase catalysis by prostaglandin-endoperoxide H synthases. Seibold SA, Ball T, Hsi LC, Mills DA, Abeysinghe RD, Micielli R, Rieke CJ, Cukier RI, Smith WL. J. Biol. Chem. 278 46163-46170 (2003)
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  33. X-ray structure of the metcyano form of dehaloperoxidase from Amphitrite ornata: evidence for photoreductive dissociation of the iron-cyanide bond. de Serrano VS, Davis MF, Gaff JF, Zhang Q, Chen Z, D'Antonio EL, Bowden EF, Rose R, Franzen S. Acta Crystallogr. D Biol. Crystallogr. 66 770-782 (2010)
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  36. The effect of myeloperoxidase isoforms on biophysical properties of red blood cells. Shamova EV, Gorudko IV, Grigorieva DV, Sokolov AV, Kokhan AU, Melnikova GB, Yafremau NA, Gusev SA, Sveshnikova AN, Vasilyev VB, Cherenkevich SN, Panasenko OM. Mol Cell Biochem 464 119-130 (2020)
  37. ESR and X-ray Structure Investigations on the Binding and Mechanism of Inhibition of the Native State of Myeloperoxidase with Low Molecular Weight Fragments. Chavali B, Masquelin T, Nilges MJ, Timm DE, Stout SL, Matter WF, Jin N, Jadhav PK, Deng GG. Appl Magn Reson 46 853-873 (2015)
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  39. DFT calculations suggest a new type of self-protection and self-inhibition mechanism in the mammalian heme enzyme myeloperoxidase: nucleophilic addition of a functional water rather than one-electron reduction. Sicking W, Somnitz H, Schmuck C. Chemistry 18 10937-10948 (2012)
  40. Design of anti-thyroid drugs: Binding studies and structure determination of the complex of lactoperoxidase with 2-mercaptoimidazole at 2.30 Å resolution. Sirohi HV, Singh PK, Iqbal N, Sharma P, Singh AK, Kaur P, Sharma S, Singh TP. Proteins 85 1882-1890 (2017)
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  44. Native glycosylation and binding of the antidepressant paroxetine in a low-resolution crystal structure of human myeloperoxidase. Krawczyk L, Semwal S, Soubhye J, Lemri Ouadriri S, Prévost M, Van Antwerpen P, Roos G, Bouckaert J. Acta Crystallogr D Struct Biol 78 1099-1109 (2022)
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  1. Structure of the green heme in myeloperoxidase.. Fenna R, Zeng J, Davey C Arch Biochem Biophys 316 653-6 (1995)
  2. 2.3 A 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.. Davey CA, Fenna RE Biochemistry 35 10967-73 (1996)
  3. X-Ray Crystal Structure of Canine Myeloperoxidase at 3 Angstrom Resolution. Zeng J, Fenna RE J. Mol. Biol. 226 185- (1992)
  4. Site-directed mutagenesis of human myeloperoxidase: further identification of residues involved in catalytic activity and heme interaction.. Jacquet A, Garcia-Quintana L, Deleersnyder V, Fenna R, Bollen A, Moguilevsky N Biochem Biophys Res Commun 202 73-81 (1994)

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