Mechanism of light-induced oxidation of nitrosylmyoglobin

Food Chemistry

Volumn 121, Issue 2, 2010, Pages 472-479

  Munk, Merete B ^a   Huvaere, Kevin ^a   Van Bocxlaer, Jan ^b   Skibsted, Leif H ^a  

^a UNIVERSITY OF COPENHAGEN   (Denmark)

^b Laboratory of Medical Biochemistry and Clinical Analysis   (Belgium)

Author keywords

Mass spectrometry; Nitrosylmyoglobin; Photodegradation

Indexed keywords

AMMONIUM ACETATE; HEME; METMYOGLOBIN; MYOGLOBIN; NITRATE; NITRIC ACID; NITRIC OXIDE; NITROSYLMYOGLOBIN; OXYGEN; PEROXYNITRITE; TRYPTOPHAN; TYROSINE; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; ELECTROSPRAY; MEAT; NITRATION; NITROSYLATION; PHOTODEGRADATION; PHOTOLYSIS; PHOTOOXIDATION;

EID: 77049101919     PISSN: 03088146     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodchem.2009.12.067     Document Type: Article

References (53)

1. Andersen H.J., and Skibsted L.H. Kinetics and mechanism of thermal oxidation and photooxidation of nitrosylmyoglobin in aqueous solution. Journal of Agricultural and Food Chemistry 40 (1992) 1741-1750
2. Antonini, E., & Brunori, M. (1971). In A. Neuberger, & E. L. Tatum (Eds.), Hemoglobin and myoglobin in their reactions with ligands, Frontiers of biology, (Vol. 21, pp. 13-39). Amsterdam: North Holland Publishing Company.
3. Arnold E.V., and Bohle D.S. Isolation and oxygenation reactions of nitrosylmyoglobins. Methods of Enzymology 269 (1996) 41-55
4. Arnold E.V., Bohle D.S., and Jordan P.A. Reversible and irreversible hemichrome generation by the oxygenation of nitrosylmyoglobin. Biochemistry 38 (1999) 4750-4756
5. Babu K.R., and Douglas D.J. Methanol-induced conformations of myoglobin at pH 4.0. Biochemistry 39 (2000) 14702-14710
6. Bourassa J.L., Ives E.P., Marqueling A.L., Shimanovich R., and Groves J.T. Myoglobin catalyzes its own nitration. Journal of the American Chemical Society 123 (2001) 5142-5143
7. Brunori M., and Gibson Q.H. Cavities and packing defects in the structural dynamics of myoglobin. EMBO Reports 2 (2001) 674-679
8. Carlsen C.U., Møller J.K.S., and Skibsted L.H. Heme-iron in lipid oxidation. Coordination Chemistry Reviews 249 (2005) 485-498
9. Carver T.E., Rohlfs R.J., Olson J.S., Gibson Q.H., Blackmore R.S., Springer B.A., et al. Analysis of the kinetic barriers for ligand binding to sperm whale myoglobin using site-directed mutagenesis and laser photolysis techniques. Journal of Biological Chemistry 265 (1990) 20007-20020
10. Cooper C.E. Nitric oxide and iron proteins. Biochimica et Biophysica Acta 1411 (1999) 290-309
11. Decatur S.M., Franzen S., DePillis G.D., Dyer R.B., Woodruff W.H., and Boxer S.G. Trans effects in nitric oxide binding to myoglobin cavity mutant H93G. Biochemistry 35 (1996) 4939-4944
12. Doyle M.P., and Hoekstra J.W. Oxidation of nitrogen-oxides by bound dioxygen in hemoproteins. Journal of Inorganic Biochemistry 14 (1981) 351-358
13. Duprat A.F., Traylor T.G., Wu G., Coletta M., Sharma V.S., Walda K.N., et al. Myoglobin-NO at low pH: Free four-coordinated heme in the protein pocket. Biochemistry 34 (1995) 2634-2644
14. Eich R.F., Li T., Lemon D.D., Doherty D.H., Curry S.R., Aitken J.F., et al. Mechanism of NO-induced oxidation of myoglobin and haemoglobin. Biochemistry 35 (1996) 6976-6983
15. Ford P.C., Wink D.A., and Stanbury D.M. Autoxidation kinetics of aqueous nitric-oxide. FEBS Letters 326 (1993) 1-3
16. {radical dot}, in the reaction between oxygen and nitric oxide in solution. Free Radical Research 27 (1997) 31-35
17. Gibson Q.H., Regan R., Elber R., Olson J.S., and Carver T.E. Distal pocket residues affect picosecond ligand recombination in myoglobin. An experimental and molecular dynamics study of position 29 mutants. Journal of Biological Chemistry 267 (1992) 22022-22034
18. {radical dot} -. Journal of Biological Chemistry 278 (2003) 50949-50955
19. Gunther M.R., Tschirret-Guth R.A., Witkowska H.E., Fann Y.C., Barr D.P., Ortiz de Montellano P.R., et al. Site-specific spin trapping of tyrosine radicals in the oxidation of metmyoglobin by hydrogen peroxide. Biochemical Journal 330 (1998) 1293-1299
20. Hatchard C.G., and Parker C.A. A new sensitive chemical actinometer. II. Potassium ferrioxalate as a standard chemical actinometer. Proceedings of the Royal Society of London A 235 (1956) 518-536
21. Herold S. Kinetic and spectroscopic characterization of an intermediate peroxynitrite complex in the nitrogen monoxide induced oxidation of oxyhemoglobin. FEBS Letters 439 (1998) 85-88
22. {radical dot}- mediated oxidation of oxymyoglobin and oxyhemoglobin. Biochemistry 40 (2001) 3385-3395
23. Herold S., Matsui T., and Watanabe Y. Peroxynitrite isomerization catalyzed by His64 myoglobin mutants. Journal of the American Chemical Society 123 (2001) 4085-4086
24. Herold S., Shivashankar K., and Mehl M. Myoglobin scavenges peroxynitrite without being significantly nitrated. Biochemistry 41 (2002) 13460-13472
25. Herold S., and Shivashankar K. Metmyoglobin and methemoglobin catalyze the isomerization of peroxynitrite to nitrate. Biochemistry 42 (2003) 14036-14046
26. Hoshino M., Laverman L., and Ford P.C. Nitric oxide complexes of metalloporphyrins: An overview of some mechanistic studies. Coordination Chemistry Reviews 187 (1999) 75-102
27. Huvaere K., Sinnaeve B., Van Bocxlaer J., and De Keukeleire D. Photooxidative degradation of beer bittering principles: Product analysis with respect to lightstruck flavour formation. Photochemical and Photobiological Sciences 3 (2004) 854-858
28. 2, NO, and isocyanides. Journal of the American Chemical Society 110 (1988) 380-387
29. Kanner J., Harel S., and Granit R. Nitric-oxide as an antioxidant. Archives of Biochemistry and Biophysics 289 (1991) 130-136
30. Kelman D.J., DeGray J.A., and Mason R.P. Reaction of myoglobin with hydrogen peroxide forms a peroxyl radical which oxidizes substrates. Journal of Biological Chemistry 269 (1994) 7458-7463
31. Kissner R., Nauser T., Bugnon P., Lye P.G., and Koppenol W.H. Formation and properties of peroxynitrite as studied by laser flash photolysis, high-pressure stopped-flow technique, and pulse radiolysis. Chemical Research in Toxicology 10 (1997) 1285-1292
32. Koppenol W.H., Moreno J.J., Pryor W.A., Ischiropoulos H., and Beckman J.S. Peroxynitrite, a cloaked oxidant formed by nitric oxide and superoxide. Chemical Research in Toxicology 5 (1992) 834-842
33. Millar S.J., Moss B.W., and Stevenson M.H. Some observation on the absorption spectra of various myoglobin derivatives found in meat. Meat Science 42 (1996) 277-288
34. Moore E.G., and Gibson Q.H. Cooperativity in the dissociation of nitric oxide from haemoglobin. Journal of Biological Chemistry 251 (1976) 2788-2794
35. Motohashi N., Mori I., Sugiura Y., and Tanaka H. Modification of γ-irradiation-induced change in myoglobin by α-mercaptopropionylglycine and its related compounds and the formation of sulfmyoglobin. Radiation Research 86 (1981) 479-487
36. Møller J.K.S., Bertelsen G., and Skibsted L.H. Photooxidation of nitrosylmyoglobin at low oxygen pressure. Quantum yields and reaction stoechiometries. Meat Science 60 (2002) 421-425
37. Møller J.K.S., Jensen J.S., Skibsted L.H., and Knöchel S. Microbial formation of nitrite-cured pigment, nitrosylmyoglobin, from metmyoglobin in model systems and smoked fermented sausages by Lactobacillus fermentum strains and a commercial starter culture. European Food Research and Technology 216 (2003) 463-469
38. Møller J.K.S., and Skibsted L.H. Mechanism of nitrosylmyoglobin autoxidation: Temperature and oxygen pressure effects on the two consecutive reactions. Chemistry - A European Journal 10 (2004) 2291-2300
39. Møller J.K.S., Nannerup L., and Skibsted L.H. Effect of carbon dioxide on autoxidation and photooxidation of nitrosylmyoglobin. Meat Science 69 (2005) 71-78
40. Møller J.K.S., and Skibsted L.H. Color. In: Toldrá F. (Ed). Handbook of fermented meat and poultry (2007), Wiley-VCH Verlag, Weinheim 203-216
41. Palmer G. Electron paramagnetic resonance of hemoproteins. In: Lever A.B.P., and Gray H.B. (Eds). Iron porphyrins, Part II (1983), Addison-Wesley Publishing Company, Massachusetts 43-88
42. Pegg R.B., and Shahidi F. Unraveling the chemical identity of meat pigments. Critical Reviews in Food Science and Nutrition 37 (1997) 561-589
43. Pietraforte D., Salzano A.M., Marino G., and Minetti M. Peroxynitrite-dependent modifications of tyrosine residues in hemoglobin. Formation of tyrosyl radical(s) and 3-nitrotyrosine. Amino Acids 25 (2003) 341-350
44. Quillin M.L., Li T., Olson J.S., Phillips Jr. G.N., Duo Y., Ikeda-Saito M., et al. Structural and functional effects of apolar mutations of the distal valine in myoglobin. Journal of Molecular Biology 245 (1995) 416-436
45. Rosen G.M., Porasuphatana S., Tsai P., Ambulos N.P., Galtsev V.E., Ichikawa K., et al. Dendrimeric-containing nitronyl nitroxides as spin traps for nitric oxide: Synthesis, kinetic, and stability studies. Macromolecules 36 (2003) 1021-1027
46. Schmidt A., and Karas M. The influence of electrostatic interactions on the detection of heme globin complexes in ESI-MS. Journal of the American Society for Mass Spectrometry 12 (2001) 1092-1098
47. Sono M., Smith P.D., McCray J.A., and Asakura T. Kinetic and equilibrium studies of the reactions of heme-substituted horse heart myoglobins with oxygen and carbon monoxide. Journal of Biological Chemistry 251 (1976) 1418-1426
48. Upmacis R.K., Hajjar D.P., Chait B.T., and Mirza U.A. Direct observation of nitrosylated heme in myoglobin and hemoglobin by electrospray ionization mass spectrometry. Journal of the American Chemical Society 119 (1997) 10424-10429
49. Van der Zee J. Formation of peroxide- and globin-derived radicals from the reaction of methaemoglobin and metmyoglobin with t-butyl hydroperoxide: an ESR spin-trapping investigation. Biochemical Journal 322 (1997) 633-639
50. Van Dyke B.R., Saltman P., and Armstrong F.A. Control of myoglobin electron-transfer rates by the distal (nonbound) histidine residue. Journal of the American Chemical Society 118 (1996) 3490-3492
51. - under argon and in air. Chemical Research in Toxicology 9 (1996) 1382-1390
52. Walsh K.A., and Rose D. Factors affecting the oxidation of nitric oxide myoglobin. Journal of Agricultural and Food Chemistry 4 (1956) 352-355
53. 2 and the vibrational relaxation of the six-coordinate heme species. Journal of the American Chemical Society 124 (2002) 5914-5924