Characterization of dehaloperoxidase compound ES and its reactivity with trihalophenols

Biochemistry

Volumn 48, Issue 5, 2009, Pages 995-1005

  Feducia, Jeremiah ^a   Dumarieh, Rania ^a   Gilvey, Lauren B G ^a   Smirnova, Tatyana ^a   Franzen, Stefan ^a   Ghiladi, Reza A ^a  

^a NORTH CAROLINA STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIFUNCTIONAL PROTEINS; CYTOCHROME C; DIOXYGEN; ELECTRON PARAMAGNETIC RESONANCE SPECTROSCOPIES; KINETIC DESCRIPTIONS; NEW SPECIES; OXYGEN TRANSPORTS; PEROXIDASE ACTIVITIES; TRICHLOROPHENOL; TYROSYL RADICALS;

BIOCHEMICAL OXYGEN DEMAND; CATALYTIC OXIDATION; DEHALOGENATION; ELECTRON SPIN RESONANCE SPECTROSCOPY; HEMOGLOBIN; HYDROGEN; HYDROGEN PEROXIDE; OXIDATION; OXYGEN; PARAMAGNETIC RESONANCE; PARAMAGNETISM; PORPHYRINS;

SUBSTRATES;

2,,4,6 TRICHLOROPHENOL; 2,4 DICHLOROQUINONE; CYTOCHROME C PEROXIDASE; DEHALOPEROXIDASE; HEME; HYDROGEN PEROXIDE; PEROXIDASE; PHENOL DERIVATIVE; TRIHALOPHENOL DERIVATIVE; UNCLASSIFIED DRUG; 2,4,6 TRICHLOROPHENOL; 2,4,6-TRICHLOROPHENOL; CHLOROPHENOL; CYTOCHROME C OXIDASE; DHP I DEHALOPEROXIDASE; HEMOGLOBIN;

ARTICLE; CATALYSIS; CHEMICAL STRUCTURE; CRYSTAL STRUCTURE; ELECTRON SPIN RESONANCE; ENZYME ACTIVITY; ENZYME MECHANISM; OXYGEN TRANSPORT; PRIORITY JOURNAL; ULTRAVIOLET SPECTROSCOPY; ANIMAL; BINDING SITE; CHEMISTRY; ENZYMOLOGY; METABOLISM; POLYCHAETA; X RAY CRYSTALLOGRAPHY;

AMPHITRITE ORNATA; POLYCHAETA; TEREBELLIDA;

ANIMALS; BINDING SITES; CHLOROPHENOLS; CRYSTALLOGRAPHY, X-RAY; CYTOCHROME-C PEROXIDASE; ELECTRON TRANSPORT COMPLEX IV; HEMOGLOBINS; PEROXIDASES; POLYCHAETA;

EID: 61449121236     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi801916j     Document Type: Article

References (45)

1. Weber, R. E., Magnum, C. P., Steinman, H., Bonaventura, C, Sullivan, B., and Bonaventura, J. (1977) Hemoglobins of two terebellid polychaetes: Enoplobranchus sanuigneus and Amphitire ornata. Comp. Biochem. Phys. 56A, 179-187.
2. Chen, Y. P., Woodin, S. A., Lincoln, D. E., and Lovell, C. R. (1996) An unusual dehalogenating peroxidase from the marine terebellid ploychaete Amphitrite ornata. J. Biol. Chem. 271, 4609-4612.
3. 2-dependent oxidative dehalogenation of chlorophenols to DNA-binding radicals and quinones. Biochemistry 46, 9823-9829.
4. Belyea, J., Gilvey, L. B., Davis, M. F., Godek, M., Sit, T. L., Lommel, S. A., and Franzen, S. (2005) Enzyme function of the globin dehaloperoxidase from Amphitrite ornata is activated by substrate binding. Biochemistry 44, 15637-15644.
5. Hardison, R. (1998) Hemoglobins from bacteria to man: Evolution of different patterns of gene expression. J. Exp. Biol. 201, 1099-1117.
6. Bailly, X., Chabasse, C, Hourdez, S., Dewilde, S., Martial, S., Moens, L., and Zal, F. (2007) Globin gene family evolution and functional diversification in annelids. FEBS J. 274, 2641-2652.
7. Franzen, S., Gilvey, L. B., and Belyea, J. L. (2007) The pH dependence of the activity of dehaloperoxidase from Amphitrite ornata. Biochim. Biophys. Acta 1774, 121-130.
8. LaCount, M. W., Zhang, E. L., Chen, Y. P., Han, K. P., Whitton, M. M., Lincoln, D. E., Woodin, S. A., and Lebioda, L. (2000) The crystal structure and amino acid sequence of dehaloperoxidase from Amphitrite ornata indicate common ancestry with globins. J. Biol. Chem. 275, 18712-18716.
9. Poulos, T. L., and Kraut, J. (1980) The structure of cytochrome c peroxidase at 2.5 Å resolution. J. Biol. Chem. 255, 575-580.
10. Akita, M., Tsutsumi, D., Kobayashi, M., and Kise, H. (2001) Structural change and catalytic activity of horseradish peroxidase in oxidative polymerization of phenol. Biosci., Biotechnol., Biochem. 65, 1581-1588.
11. Laurenti, E., Ghibaudi, E., Todaro, G., and Ferrari, R. P. (2002) Enzymatic degradation of 2,6-dichlorophenol by horseradish peroxidase: UV-visible and mass spectrophotometric characterization of the reaction products. J. Inorg. Biochem. 92, 75-81.
12. Laurenti, E., Ghibaudi, E., Ardissone, S., and Ferrari, R. P. (2003) Oxidation of 2,4-dichlorophenol catalyzed by horseradish peroxidase: Characterization of the reaction mechanism by UV-visible spectroscopy and mass spectrometry. J. Inorg. Biochem. 95, 171-176.
13. Raven, E. L. (2000) Peroxidase-Catalyzed Oxidation of Ascorbate. In Subcellular Chemistry, Volume 35: Enzyme-Catalyzed Electron and Radical Transfer (Holzenburg, A., and Scrutton, N, Eds.) pp 317-349, Kluwer Academic/Plenum Publishers, New York.
14. Neely, W. B. (1984) An Analysis of Aquatic Toxicity Data: Water Solubility and Acute Lc50 Fish Data. Chemosphere 13, 813-819.
15. Dannenfelser, R. M., and Yalkowsky, S. H. (1991) Data-Base of Aqueous Solubility for Organic Nonelectrolytes. Sci. Total EnViron. 109, 625-628.
16. Falk, J. E. (1964) Haems. I. Determination as pyridine hemo-chromes. Porphyrins and Metalloporphyrins: Their General, Physical, and Coordination Chemistry and Laboratory Methods, pp 181 - 188, Elsevier Publishing, New York.
17. Fuhrhop, J. H., and Smith, K. M. (1975) Laboratory Methods. In Porphyrins and Metalloporphyrins (Smith, K. M., Ed.) pp 804-807, Elsevier Publishing, New York.
18. Beers, R. F., Jr., and Sizer, I. W. (1952) A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase. J. Biol. Chem. 195, 133-140.
19. Osborne, R. L., Taylor, L. O., Han, K. P., Ely, B., and Dawson, J. H. (2004) Amphitrite ornata dehaloperoxidase: Enhanced activity for the catalytically active globin using MCPBA. Biochem. Biophys. Res. Commun. 324, 1194-1198.
20. Nienhaus, K., Deng, P. C, Belyea, J., Franzen, S., and Nienhaus, G. U. (2006) Spectroscopic study of substrate binding to the carbonmonoxy form of dehaloperoxidase from Amphitrite ornata. J. Phys. Chem. B 110, 13264-13276.
21. Davis, M. F., Gracz, H, Vendeix, F. A. P., Gilvey, L. B., Somasundaram, A., Decatur, S. M., and Franzen, S. (2009) Different Binding Modes of Mono-, Di- and Trihalogenated Phenols to the Hemoglobin Dehaloperoxidase from Amphitrite ornata. Biochemistry . (submitted for publication).
22. Franzen, S., Chaudhary, C, Belyea, J., Gilvey, L., Davis, M. F., Sit, T. L., and Lommel, S. A. (2006) Proximal cavity, distal histidine and substrate hydrogen-bonding mutations modulate the activity of Amphitrite ornata dehaloperoxidase. Biochemistry 45, 9085-9094.
23. Svistunenko, D. A., and Cooper, C. E. (2004) A new method of identifying the site of tyrosyl radicals in proteins. Biophys. J. 87, 582-595.
24. Svistunenko, D. A., Dunne, J., Fryer, M., Nicholls, P., Reeder, B. J., Wilson, M. T., Bigotti, M. G, Cutruzzola, F., and Cooper, C. E. (2002) Comparative study of tyrosine radicals in hemoglobin and myoglobins treated with hydrogen peroxide. Biophys. J. 83, 2845-2855.
25. Lawrence, C. C, Bennati, M., Obias, H. V., Bar, G., Griffin, R. G., and Stubbe, J. (1999) High-field EPR detection of a disulfide radical anion in the reduction of cytidine 5'-diphosphate by the E441Q R1 mutant of Escherichia coli ribonucleotide reductase. Proc. Natl. Acad. Sci. U.S.A. 96, 8979-8984.
26. Hoffman, M. Z., and Hayon, E. (1972) One-Electron Reduction of Disulfide Linkage in Aqueous-Solution: Formation, Protonation, and Decay Kinetics of RSSR- Radical. J. Am. Chem. Soc. 94, 7950-7957.
27. Chan, P. C, and Bielski, B. H. J. (1973) Pulse-Radiolysis Study of Optical-Absorption and Kinetic Properties of Dithiothreitol Free-Radical. J. Am. Chem. Soc. 95, 5504-5508.
28. Witting, P. K, Douglas, D. J., and Mauk, A. G (2000) Reaction of human myoglobin and H2O2: Involvement of a thiyl radical produced at cysteine 110. J. Biol. Chem. 275, 20391-20398.
29. Svistunenko, D. A. (2005) Reaction of haem containing proteins and enzymes with hydroperoxides: The radical view. Biochim. Biophys. Acta 1707, 127-155.
30. Lund, M. N, Luxford, C, Skibsted, L. H., and Davies, M. J. (2008) Oxidation of myosin by haem proteins generates myosin radicals and protein cross-links. Biochem. J. 410, 565-574.
31. Roach, M. P., Chen, Y. P., Woodin, S. A., Lincoln, D. E., and Dawson, J. H. (1997) Notomastus lobatus chloroperoxidase and Amphitrite ornata dehaloperoxidase both contain histidine as their proximal heme iron ligand. Biochemistry 36, 2197-2202.
32. Davydov, R., Osborne, R. L., Kim, S. H., Dawson, J. H., and Hoffman, B. M. (2008) EPR and ENDOR studies of cryoreduced compounds II of peroxidases and myoglobin. Proton-coupled electron transfer and protonation status of ferryl. Biochemistry 47, 5147-5155.
33. 2 reaction. J. Am. Chem. Soc. 118, 12236-12237.
34. Hirota, S., Azuma, K., Fukuba, M., Kuroiwa, S., and Funasaki, N. (2005) Heme reduction by intramolecular electron transfer in cysteine mutant myoglobin under carbon monoxide atmosphere. Biochemistry 44, 10322-10327.
35. Smith, A. T., and Veitch, N. C. (1998) Substrate binding and catalysis in heme peroxidases. Curr. Opin. Chem. Biol. 2, 269-278.
36. Witting, P. K., Mauk, A. G., and Lay, P. A. (2002) Role of tyrosine-103 in myoglobin peroxidase activity: Kinetic and steady-state studies on the reaction of wild-type and variant recombinant human myoglobins with H2O2. Biochemistry 41, 11495-11503.
37. Smirnova, T. I., Weber, R. T., Davis, M. F., and Franzen, S. (2008) Substrate binding triggers a switch in the iron coordination in dehaloperoxidase from Amphitrite ornata: HYSCORE experiments. J. Am. Chem. Soc. 130, 2128-2129.
38. Gajhede, M. (2001) Horseradish Peroxidase. In Handbook of Metalloprotein (Messerschmidt, A., Huber, R., Poulos, T. L., and Weighardt, K., Eds.) pp 195-210, John Wiley & Sons, Inc., Chichester, U.K.
39. Keilin, D., and Hartree, E. F. (1950) Reaction of Methaemoglobin with Hydrogen Peroxide. Nature 166, 513-514.
40. George, P., and Irvine, D. H. (1951) Reaction of Metmyoglobin with Hydrogen Peroxide. Nature 168, 164-165.
41. Giulivi, C., and Cadenas, E. (1998) Heme protein radicals: Formation, fate, and biological consequences. Free Radical Biol. Med. 24, 269-279.
42. Alayash, A. I., Ryan, B. A. B., Eich, R. F., Olson, J. S., and Cashon, R. E. (1999) Reactions of sperm whale myoglobin with hydrogen peroxide: Effects of distal pocket mutations on the formation and stability of the ferryl intermediate. J. Biol. Chem. 274, 2029-2037.
43. Wood, Z. A., Schroder, E., Harris, J. R., and Poole, L. B. (2003) Structure, mechanism and regulation of peroxiredoxins. Trends Biochem. Sci. 28, 32-40.
44. Niviere, V., and Fontecave, M. (2004) Discovery of superoxide reductase: An historical perspective. J. Biol. Inorg. Chem. 9, 119-123.
45. Dunford, H. B. (1999) Heme Peroxidases, Wiley-VCH, New York (and references cited therein).