Arthromyces ramosus peroxidase produces two chlorinating species

Biochemical and Biophysical Research Communications

Volumn 355, Issue 2, 2007, Pages 581-586

  Huang, Liusheng ^a   Ortiz de Montellano, Paul R ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Arthromyces ramosus peroxidase; Chloride oxidation; Chloride radical; Heme modification; Horseradish peroxidase; Hypochloric acid; Monochlorodimedone

Indexed keywords

HEME; PEROXIDASE;

ARTHROMYCES RAMOSUS; ARTICLE; CHLORINATION; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME MODIFICATION; ENZYME STRUCTURE; HYPHOMYCETES; NONHUMAN; PH; PRIORITY JOURNAL;

CHLORINE; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; FUNGI; HEME; HYDROGEN-ION CONCENTRATION; MASS SPECTROMETRY; OXIDATION-REDUCTION; PEROXIDASES;

'ARTHROMYCES RAMOSUS'; ARMORACIA RUSTICANA;

EID: 33847110239     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2007.02.016     Document Type: Article

References (31)

1. Raven E.L. Understanding functional diversity and substrate specificity in haem peroxidases: what can we learn from ascorbate peroxidase?. Nat. Prod. Rep. 20 (2003) 367-381
2. Veitch N.C. Horseradish peroxidase: a modern view of a classic enzyme. Phytochemistry 65 (2004) 249-259
3. Furtmüller P.G., Zederbauer M., Jantschko W., Helm J., Bogner M., Jakopitsch C., and Obinger C. Active site structure and catalytic mechanisms of human peroxidases. Arch. Biochem. Biophys. 445 (2006) 199-213
4. Vlasova I.I., Arnhold J., Osipov A.N., and Panasenko O.M. pH-Dependent regulation of myeloperoxidase activity. Biochemistry (Moscow) 71 (2006) 667-677
5. Hurst J.K., and Barrette Jr. W.C. Leukocyte oxygen activation and microbicidal oxidative toxins. CRC Crit. Rev. Biochem. Mol. Biol. 24 (1989) 271-328
6. Dunford H.B. Horseradish peroxidase. I: ligand binding, redox potentials, formation of its compounds, and some of their reactions. Heme Peroxidases (1999), Springer, NY pp. 58-91
7. Dunford H.B. Chloroperoxidase and Pseudomonas cytochrome c peroxidase. Heme Peroxidases (1999), Wiley-VCH, NY pp. 323-385
8. Gaut J.P., Yeh G.C., Tran H.D., Byun J., Henderson J.P., Richter G.M., Brennan M.L., Lusis A.J., Belaaouaj A., Hotchkiss R.S., and Heinecke J.W. Neutrophils employ the myeloperoxidase system to generate antimicrobial brominating and chlorinating oxidants during sepsis. Proc. Natl. Acad. Sci. USA 98 (2001) 11961-11966
9. Marquez L.A., and Dunford H.B. Chlorination of taurine by myeloperoxidase. Kinetic evidence for an enzyme-bound intermediate. J. Biol. Chem. 269 (1994) 7950-7956
10. Woggon W.D., Wagenknecht H.A., and Claude C. Synthetic active site analogues of heme-thiolate proteins. Characterization and identification of intermediates of the catalytic cycles of cytochrome P450cam and chloroperoxidase. J. Inorg. Biochem. 83 (2001) 289-300
11. Manoj K.M. Chlorinations catalyzed by chloroperoxidase occur via diffusible intermediate(s) and the reaction components play multiple roles in the overall process. Biochim. Biophys. Acta 1764 (2006) 1325-1339
12. Lambeir A.-M., and Dunford H.B. A steady state kinetic analysis of the reaction of chloroperoxidase with peracetic acid, chloride, and 2-chlorodimedone. J. Biol. Chem. 258 (1983) 13558-13563
13. Huang L., and Ortiz de Montellano P.R. Heme-protein covalent bonds in peroxidases and resistance to heme modification during halide oxidation. Arch. Biochem. Biophys. 446 (2006) 77-83
14. Huang L., Wojciechowski G., and Ortiz de Montellano P.R. Prosthetic heme modification during halide ion oxidation. Demonstration of chloride oxidation by horseradish peroxidase. J. Am. Chem. Soc. 127 (2005) 5345-5353
15. Furtmüller P.G., Jantschko W., Regelsberger G., Jakopitsch C., Arnhold J., and Obinger C. Reaction of lactoperoxidase compound I with halides and thiocyanate. Biochemistry 41 (2002) 11895-11900
16. Wojciechowski G., Huang L., and Ortiz de Montellano P.R. Autocatalytic modification of the prosthetic heme of horseradish but not lactoperoxidase by thiocyanate oxidation products. A role for heme-protein covalent crosslinking. J. Am. Chem. Soc. 127 (2005) 15871-15879
17. Ohlsson P.I., and Paul K. Horseradish peroxidase with 2,4-modified hematins, including vinyl homologues. Biochim. Biophys. Acta 315 (1973) 293-305
18. Farhangrazi Z.S., Copeland B.R., Nakayama T., Amachi T., Yamazaki I., and Powers L.S. Oxidation-reduction properties of compounds I and II of Arthromyces ramosus peroxidase. Biochemistry 33 (1994) 5647-5652
19. Hildebrandt A.G., Roots I., Tjoe M., and Heinemeyer G. Hydrogen peroxide in hepatic microsomes. Methods Enzymol. 52 (1978) 342-350
20. Ortiz de Montellano P.R. Control of the catalytic activity of prosthetic heme by the structure of hemoproteins. Accts. Chem. Res. 20 (1987) 289-294
21. Gajhede M., Schuller D.J., Henriksen A., Smith A.T., and Poulos T.L. Crystal structure of horseradishperoxidase C at 2.15 Å resolution. Nature Struct. Biol. 4 (1997) 1032-1038
22. Sharp K.H., Mewies M., Moody P.C.E., and Raven E.L. Crystal structure of the ascorbate peroxidase-ascorbate complex. Nature Struct. Biol. 10 (2003) 303-307
23. Ortiz de Montellano P.R. Free radical modification of prosthetic heme groups. Pharmac. Ther. 48 (1990) 95-120
24. Berglund G., Carlsson G., Smith A., Szoke H., Henrikson A., and Hajdu J. The catalytic pathway of horseradish peroxidase at high resolution. Nature 417 (2002) 463-468
25. 127I NMR spectroscopy, and steady-state kinetics. J. Biol. Chem. 272 (1997) 5752-5756
26. Fukuyama K., Kunishima N., Amada F., Kubota T., and Matsubara H. Crystal structures of cyanide- and triiodide-bound forms of Arthromyces ramosus peroxidase at different pH values. Perturbations of active site residues and their implication in enzyme catalysis. J. Biol. Chem. 270 (1995) 21884-21892
27. 2+ couple in Arthromyces ramosus class II peroxidase and its cyanide adduct. J. Biol. Inorg. Chem. 11 (2006) 586-592
28. Nakayama T., and Amachi T. Fungal peroxidase: its structure, function, and application. J. Mol. Catal. B: Enzymatic 6 (1999) 185-198
29. Wojciechowski G., and Ortiz de Montellano P.R. Radical energies and the regiochemistry of addition to heme groups. Methylperoxy and nitrite radical additions to heme of horseradish peroxidase. J. Am. Chem. Soc. 129 (2007) 1663
30. Berkowitz J., Ellison G.B., and Gutman D. Three methods to measure RH bond energies. J. Phys. Chem. 98 (1994) 2744-2765
31. Kumar D., de Visser S.P., and Shaik S. Theory favors a stepwise mechanism of porphyrin degradation by a ferric hydroperoxide model of the active species of heme oxygenase. J. Am. Chem. Soc. 127 (2005) 8204-8213