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Biochemistry (Moscow)

, Volume 81, Issue 13, pp 1735–1753 | Cite as

Hemoglobin and myoglobin as reducing agents in biological systems. Redox reactions of globins with copper and iron salts and complexes

  • G. B. PostnikovaEmail author
  • E. A. Shekhovtsova
Review

Abstract

In addition to reversible O2 binding, respiratory proteins of the globin family, hemoglobin (Hb) and myoglobin (Mb), participate in redox reactions with various metal complexes, including biologically significant ones, such as those of copper and iron. HbO2 and MbO2 are present in cells in large amounts and, as redox agents, can contribute to maintaining cell redox state and resisting oxidative stress. Divalent copper complexes with high redox potentials (E 0, 200-600 mV) and high stability constants, such as [Cu(phen)2]2+, [Cu(dmphen)2]2+, and CuDTA oxidize ferrous heme proteins by the simple outer-sphere electron transfer mechanism through overlapping π-orbitals of the heme and the copper complex. Weaker oxidants, such as Cu2+, CuEDTA, CuNTA, CuCit, CuATP, and CuHis (E 0≤ 100-150 mV) react with HbO2 and MbO2 through preliminary binding to the protein with substitution of the metal ligands with protein groups and subsequent intramolecular electron transfer in the complex (the site-specific outer-sphere electron transfer mechanism). Oxidation of HbO2 and MbO2 by potassium ferricyanide and Fe(3) complexes with NTA, EDTA, CDTA, ATP, 2,3-DPG, citrate, and pyrophosphate PPi proceeds mainly through the simple outer-sphere electron transfer mechanism via the exposed heme edge. According to Marcus theory, the rate of this reaction correlates with the difference in redox potentials of the reagents and their self-exchange rates. For charged reagents, the reaction may be preceded by their nonspecific binding to the protein due to electrostatic interactions. The reactions of LbO2 with carboxylate Fe complexes, unlike its reactions with ferricyanide, occur via the site-specific outer-sphere electron transfer mechanism, even though the same reagents oxidize structurally similar MbO2 and cytochrome b 5 via the simple outer-sphere electron transfer mechanism. Of particular biological interest is HbO2 and MbO2 transformation into met-forms in the presence of small amounts of metal ions or complexes (catalysis), which, until recently, had been demonstrated only for copper compounds with intermediate redox potentials. The main contribution to the reaction rate comes from copper binding to the “inner” histidines, His97 (0.66 nm from the heme) that forms a hydrogen bond with the heme propionate COO group, and the distal His64. The affinity of both histidines for copper is much lower than that of the surface histidines residues, and they are inaccessible for modification with chemical reagents. However, it was found recently that the high-potential Fe(3) complex, potassium ferricyanide (400 mV), at a 5 to 20% of molar protein concentration can be an efficient catalyst of MbO2 oxidation into metMb. The catalytic process includes binding of ferrocyanide anion in the region of the His119 residue due to the presence there of a large positive local electrostatic potential and existence of a “pocket” formed by Lys16, Ala19, Asp20, and Arg118 that is sufficient to accommodate [Fe(CN)6]4–. Fast, proton-assisted reoxidation of the bound ferrocyanide by oxygen (which is required for completion of the catalytic cycle), unlike slow [Fe(CN)6]4– oxidation in solution, is provided by the optimal location of neighboring protonated His113 and His116, as it occurs in the enzyme active site.

Keywords

hemoglobin myoglobin leghemoglobin copper and iron salts and complexes redox reactions electrostatic potential 

Abbreviations

Hb

hemoglobin

Lb

leghemoglobin

Mb

myoglobin

MbO2

oxymyoglobin

metMb

metmyoglobin

bipy

4,4′-bipyridine

CA-Mb

metmyoglobin carboxyamidated at histidine residues

CDTA

trans-1,2-diaminocyclohexane-N,N,N′,N′-tetraacetic acid

Cit

citrate

CM-Mb

metmyoglobin carboxymethylated at histidine residues

dmphen

2,9-dimethyl-1,10-phenanthroline

2,3-DPG

2,3-diphosphoglycerate

DTA

2,5-dithiohexane-1,6-dicarboxylate

EDTA

ethylenediaminetetraacetic acid

EP

electrostatic potential

NTA

nitrilotriacetic acid

phen

1,10-phenanthroline

PPi

pyrophosphate

ROS

reactive oxygen species

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References

  1. 1.
    Antonin, E., and Brunori, M. (1971) Hemoglobin and Myoglobin in Their Reactions with Ligands, in Frontiers in Biology, Amsterdam-London, p. 405.Google Scholar
  2. 2.
    Arutyunyan, E. G., Safonova, T. N., Obmolova, G. V., Teplyakov, A. V., Popov, A. N., Rusakov, A. A., Rubinskii, S. V., Kuranova, I. P., and Vainshtein, B. K. (1990) Crystal structure of oxyleghemoglobin at a 1.7 Å resolution, Bioorg. Khim., 16, 293–302.Google Scholar
  3. 3.
    Shikama, K. (1998) The molecular mechanism of autoxidation for myoglobin and hemoglobin: a venerable puzzle, Chem. Rev., 98, 1357–1373.CrossRefPubMedGoogle Scholar
  4. 4.
    Brantley, R. E., Smerdon, S. J., Wilkinson, A. J., Singleton, E. W., and Olson, J. S. (1993) The mechanism of autooxidation of myoglobin, J. Biol. Chem., 268, 6995–7010.PubMedGoogle Scholar
  5. 5.
    Allen, K. E., and Cornforth, D. P. (2006) Myoglobin oxidation in a model system as affected by nonheme iron and chelating agents, J. Agric. Food Chem., 54, 10134–10140.CrossRefPubMedGoogle Scholar
  6. 6.
    Augustin, M. A., and Yandell, J. K. (1979) Oxidation of heme proteins by copper(II) complexes. Rates and mechanism of the copper catalyzed autoxidation of cytochrome c, myoglobin and hemoglobin, Inorg. Chim. Acta, 37, 11–18.CrossRefGoogle Scholar
  7. 7.
    Eguchi, L. A., and Saltman, P. (1984) The aerobic reduction of Fe(III) complexes by hemoglobin and myoglobin, J. Biol. Chem., 259, 14337–14338.PubMedGoogle Scholar
  8. 8.
    Hegetschweiler, K., Saltman, P., Dalvit, C., and Wright, P. E. (1987) Kinetics and mechanisms of the oxidation of myoglobin by Fe(III) and Cu(II) complexes, Biochim. Biophys. Acta, 912, 384–397.CrossRefPubMedGoogle Scholar
  9. 9.
    Eguchi, L. A., and Saltman, P. (1987) Kinetics and mechanisms of metal reduction by hemoglobin. 2. Reduction of copper(II) complexes, Inorg. Chem., 26, 3669–3672.CrossRefGoogle Scholar
  10. 10.
    Hura, C., Palamaru, I., and Hura, B. (2002) Assessment of some heavy metals in the maternal body, risk in cancer disease, in Metal Ions in Biology and Medicine: Proc. 7th Int. Symp. on Metal Ions in Biology and Medicine (Khassanova, L., Collery, Ph., Maymard, I., Khassanova, Z., and Etienne, J.-C., eds.) John Libbey Eurotext, St. Petersburg, Vol. 7, pp. 621–624.Google Scholar
  11. 11.
    Mauk, M. R., Rosell, F. I., and Mauk, A. G. (2009) Metal ion facilitated dissociation of heme from b-type heme proteins, J. Am. Chem. Soc., 131, 16976–16983.CrossRefPubMedGoogle Scholar
  12. 12.
    Clopton, D. A., and Saltman, P. (1997) Copper-specific damage in human erythrocytes exposed to oxidative stress, Biol. Trace Elem. Res., 56, 231–240.CrossRefPubMedGoogle Scholar
  13. 13.
    Gunther, M. R., Sampath, V., and Caughey, W. S. (1999) Potential roles of myoglobin autoxidation in myocardial ischemia-reperfusion injury, Free Radic. Biol. Med., 26, 1388–1395.CrossRefPubMedGoogle Scholar
  14. 14.
    Stadtman, E. R., and Oliver, C. N. (1991) Metal-catalyzed oxidation of proteins, J. Biol. Chem., 266, 2005–2008.PubMedGoogle Scholar
  15. 15.
    Van Dyke, B. R., and Saltman, P. (1996) Hemoglobin: a mechanism for the generation of hydroxyl radicals, Free Radic. Biol. Med., 20, 985–989.CrossRefPubMedGoogle Scholar
  16. 16.
    Sievers, G., and Ronnberg, M. (1978) Study of the pseudoperoxidative activity of soybean leghemoglobin and sperm whale myoglobin, Biochim. Biophys. Acta, 533, 293–301.CrossRefPubMedGoogle Scholar
  17. 17.
    Puppo, A., Rigaud, G., Job, D., Ricard, G., and Zeba, B. (1980) Peroxidase content of soybean root nodules, Biochim. Biophys. Acta, 614, 303–312.CrossRefPubMedGoogle Scholar
  18. 18.
    Flogel, U., Godecke, A., Klotz, L.-O., and Schrader, J. (2004) Role of myoglobin in the antioxidant defense of the heart, FASEB J., 18, 1156–1158.PubMedGoogle Scholar
  19. 19.
    Widmer, C. C., Pereira, C. P., Gehrig, P., Vallelian, F., Schoedon, G., Buehler, P. W., and Schaer, D. (2010) Hemoglobin can attenuate hydrogen peroxide-induced oxidative stress by acting as an antioxidative peroxidase, Antioxid. Redox Signal., 12, 185–198.CrossRefPubMedGoogle Scholar
  20. 20.
    Arihara, K., Cassens, R. G., Greaser, M. L., Luchansky, J. B., and Mozdziak, P. E. (1995) Localization of metmyoglobin-reducing enzyme (NADH-cytochrome b5 reductase) system components in bovine skeletal muscle, Meat Sci., 39, 205–213.CrossRefPubMedGoogle Scholar
  21. 21.
    Topunov, A. F., Melik-Sarkisyan, S. S., Lysenko, L. A., Karpilenko, G. P., and Kretovich, V. L. (1980) Properties of metleghemoglobin reductase from lupine root nodules, Biokhimiya, 45, 2053–2058.Google Scholar
  22. 22.
    Topunov, A. F., and Golubeva, L. I. (1989) Reductases reducing oxygen-transporting hemoproteins: hemoglobin, myoglobin, and leghemoglobin, Usp. Biol. Khim., 30, 239–252.Google Scholar
  23. 23.
    Zhang, B.-J., Smerdon, S. J., Wilkinson, A. J., and Sykes, A. G. (1992) Oxidation of residue 45 mutant forms of pig deoxymyoglobin with [Fe(CN)6]3–, J. Inorg. Biochem., 48, 79–84.CrossRefPubMedGoogle Scholar
  24. 24.
    Dunn, C. J., Rohlfs, R. J., Fee, J. A., and Saltman, P. (1999) Oxidation of deoxymyoglobin by [Fe(CN)6]3–, J. Inorg. Biochem., 75, 241–244.CrossRefPubMedGoogle Scholar
  25. 25.
    Marcus, R. A., and Sutin, N. (1985) Electron transfers in chemistry and biology, Biochim. Biophys. Acta, 811, 265–322.CrossRefGoogle Scholar
  26. 26.
    Margalit, R., Pecht, I., and Gray, H. B. (1983) Oxidationreduction catalytic activity of a pentaammineruthenium (III) derivative of sperm whale myoglobin, J. Amer. Chem. Soc., 105, 301–302.CrossRefGoogle Scholar
  27. 27.
    Reid, L. S., Gray, H. B., Dalvit, C., Wright, P. E., and Saltman, P. (1987) Electron transfer from cytochrome b5 to iron and copper complexes, Biochemistry, 26, 7102–7107.CrossRefPubMedGoogle Scholar
  28. 28.
    Rifkind, J. M. (1974) Copper and the autoxidation of hemoglobin, Biochemistry, 13, 2475–2481.CrossRefPubMedGoogle Scholar
  29. 29.
    Khristova, P. K., Devedzhiev, Ya. D., Atanasov, B. P., and Volkenshtein, M. V. (1980) Studies of electron transfer in hemoproteins. IV. Sperm whale oxymyoglobin oxidation catalyzed by copper ions, Mol. Biol. (Moscow), 14, 1088–1097.Google Scholar
  30. 30.
    Postnikova, G. B., Moiseeva, S. A., and Shekhovtsova, E. A. (2010) The main role of inner histidines in the molecular mechanism of myoglobin oxidation catalyzed by copper compounds, Inorg. Chem., 49, 1347–1354.CrossRefPubMedGoogle Scholar
  31. 31.
    Rifkind, J. M., Lauer, L. D., Chiang, S. C., and Li, N. C. (1976) Copper and the oxidation of hemoglobin: a comparison of horse and human hemoglobins, Biochemistry, 15, 5337–5343.CrossRefPubMedGoogle Scholar
  32. 32.
    Moiseeva, S. A., Postnikova, G. B., and Sivozhelezov, V. S. (2000) Sperm whale oxymyoglobin oxidation catalyzed by ferrocyanide ions: kinetics and mechanism, Biophysics (Moscow), 45, 988–997.Google Scholar
  33. 33.
    Moiseeva, S. A., Postnikova, G. B., and Sivozhelezov, V. S. (2001) Kinetics and mechanism of oxymyoglobin oxidation catalyzed by potassium ferrocyanide, J. Phys. Chem. (Moscow), 75, 1504–1510.Google Scholar
  34. 34.
    Hughes, M. N. (1981) The Inorganic Chemistry of Biological Processes, Wiley, New York, pp. 125–187.Google Scholar
  35. 35.
    Martell, A. E. (1982) Critical Stability Constants, Plenum, New York, pp. 1–5.CrossRefGoogle Scholar
  36. 36.
    Martell, A. E. (1981) Development of Iron Chelators for Clinical Use (Martell, A. E., Anderson, W. F., and Badman, D. G., eds.) Elsevier, New York, p. 67.Google Scholar
  37. 37.
    Buckingham, D. A., and Sargeson, A. M. (1964) Chelating Agents and Metal Chelated (Dwyer, F. P., and Mellor, D. P., eds.) Academic Press, New York, p. 237.Google Scholar
  38. 38.
    Garvan, F. L. (1964) Chelating Agents and Metal Chelated (Dwyer, F. P., and Mellor, D. P., eds.) Academic Press, New York, p. 283.Google Scholar
  39. 39.
    Rifkind, J. M. (1981) Copper and the oxidation of hemoglobin, in Metal Ions in Biological Systems (Sigel, H., and Dekker, M., eds.) New York, Vol. 12, pp. 192–232.Google Scholar
  40. 40.
    Rifkind, J. M. (1979) Oxidation of (horse) hemoglobin by copper: an intermediate detected by electron spin resonance, Biochemistry, 18, 3860–3865.CrossRefPubMedGoogle Scholar
  41. 41.
    Winterbourn, C. C., and Carrell, R. W. (1977) Oxidation of human hemoglobin by copper. Mechanism and suggested role of the thiol group of residue β-93, Biochem. J., 165, 141–148.CrossRefPubMedPubMedCentralGoogle Scholar
  42. 42.
    Banaszak, L. J., Watson, H. C., and Kendrew, J. C. (1965) The binding of cupric and zinc ions to crystalline sperm whale myoglobin, J. Mol. Biol., 12, 130–137.CrossRefPubMedGoogle Scholar
  43. 43.
    Breslow, E., and Gurd, F. R. N. (1963) Interaction of cupric and zinc ions with sperm whale metmyoglobin, J. Biol. Chem., 238, 1332–1342.PubMedGoogle Scholar
  44. 44.
    Bakan, D. A., Saltman, P., Theriault, Y., and Wright, P. E. (1991) Kinetics and mechanisms of reduction of Cu(2) and Fe(3) complexes by soybean leghemoglobin α, Biochim. Biophys. Acta, 1079, 182–196.CrossRefPubMedGoogle Scholar
  45. 45.
    Jameson, R. F. (1981) Coordination chemistry of copper with regard to biological systems, in Metal Ions in Biological Systems (Sigel, H., ed.) Marcel Dekker, New York, pp. 1–30.Google Scholar
  46. 46.
    Postnikova, G. B., and Tselikova, S. V. (1987) Electron transfer in hemoproteins. IX. The effect of zinc ions on the rate of oxymyoglobin oxidation by ferricytochrome c, Mol. Biol. (Moscow), 21, 1040–1049.Google Scholar
  47. 47.
    Shekhovtsova, E. A., and Postnikova, G. B. (2008) Mechanism of oxymyoglobin oxidation by coper ions: myoglobins carboxymethylated and carboxyamidated at histidine residues, Biophysics (Moscow), 53, 562–572.Google Scholar
  48. 48.
    Cocco, M. J., Kao, Y. H., Phillips, A. T., and Lecomte, J. T. J. (1992) Structural comparison of apomyoglobin and metaquomyoglobin: pH titration of histidines by NMR spectroscopy, Biochemistry, 31, 6481–6491.CrossRefPubMedGoogle Scholar
  49. 49.
    Bashford, D., Case, D. A., Dalvit, C., Tennant, L., and Wright, P. E. (1993) Electrostatic calculations of side-chain pK values in myoglobin and comparison with NMR data for histidines, Biochemistry, 32, 8045–8056.CrossRefPubMedGoogle Scholar
  50. 50.
    Carver, J. A., and Bradbury, J. H. (1984) Assignment of 1H NMR resonances of histidine and other aromatic residues in met-, cyano-, oxy- and (carbon monoxy)myoglobins, Biochemistry, 23, 4890–4905.CrossRefPubMedGoogle Scholar
  51. 51.
    Zhang, L., Mei, Y., Zhang, Yu., Li, S., Sun, X., and Zhu, L. (2003) Regioselective cleavage of myoglobin with copper(2) compounds at neutral pH, Inorg. Chem., 42, 492–498.CrossRefPubMedGoogle Scholar
  52. 52.
    Kent, M. S., Yim, H., and Sasaki, D. Y. (2005) Adsorption of myoglobin to Cu(2)-IDA and Ni(2)-IDA functionalized Langmuir monolayers: study of the protein layer structure during the adsorption process by neutron and X-ray reflectivity, Langmuir, 21, 6815–6824.CrossRefPubMedGoogle Scholar
  53. 53.
    Van Dyke, B. R., Bakan, D. A., Glover, K. A. M., Hegenauer, J. C., Saltman, P., Springer, B. A., and Sligar, S. G. (1992) Site-directed mutagenesis of histidine residues involved in Cu(II) binding and reduction by sperm whale myoglobin, Proc. Natl. Acad. Sci. USA, 89, 8016–8019.CrossRefPubMedPubMedCentralGoogle Scholar
  54. 54.
    Moiseeva, S. A., and Postnikova, G. B. (2001) Mechanism of oxidation of oxymyoglobin by copper ions: comparison of sperm whale, horse, and pig myoglobins, Biochemistry (Moscow), 66, 780–787.CrossRefGoogle Scholar
  55. 55.
    Rousseaux, J., Dautrevaux, M., and Han, K. (1976) Comparison of the amino acid sequence of pig heart myoglobin with other ungulate myoglobins, Biochim. Biophys. Acta, 439, 55–62.CrossRefPubMedGoogle Scholar
  56. 56.
    Goraev, E. V., Postnikova, G. B., Moiseeva, S. A., and Shekhovtsova, E. A. (2002) Oxidation of respiratory proteins by metals. Catalytic oxidation of oxymyoglobin by copper ions: kinetics and mechanism, in Metal Ions in Biology and Medicine: Proc. Seventh Int. Symp. on Metal Ions in Biology and Medicine (Khassanova, L., Collery, Ph., Maymard, I., Khassanova, Z., and Etienne, J.-C., eds.) John Libbey Eurotext, St. Petersburg, Vol. 7, pp. 68–72.Google Scholar
  57. 57.
    Gray, R. D. (1969) The kinetics of oxidation of copper(I) by molecular oxygen in perchloric acid-acetonitrile solution, J. Amer. Chem. Soc., 91, 56–62.CrossRefGoogle Scholar
  58. 58.
    Antonini, E., Brunori, M., and Wyman, J. (1965) Studies on the oxidation-reduction potentials of heme proteins. IV. The kinetics of oxidation of hemoglobin and myoglobin by ferricyanide, Biochemistry, 4, 545–551.CrossRefPubMedGoogle Scholar
  59. 59.
    Brunori, M., Saggese, U., Rotilio, G. C., Antonini, E., and Wyman, J. (1971) Redox equilibrium of sperm-whale myoglobin, Aplysia myoglobin, and Chironomus thummi hemoglobin, Biochemistry, 10, 1604–1609.CrossRefPubMedGoogle Scholar
  60. 60.
    Zhang, B. J., Andrew, C. R., Tomkinson, N. P., and Sykes, A. G. (1992) Reactivity patterns for redox reactions of monomer forms of myoglobin, hemocyanin and hemerythrin, Biochim. Biophys. Acta, 1102, 245–252.CrossRefPubMedGoogle Scholar
  61. 61.
    Colotti, G., Verzili, D., Boffi, A., and Chiancone, E. (1994) Identification of the site of ferrocyanide binding involved in the intramolecular electron transfer process to oxidized heme in Scapharca dimeric hemoglobin, Arch. Biochem. Biophys., 311, 103–106.CrossRefPubMedGoogle Scholar
  62. 62.
    Egyed, A., May, A., and Jacobs, A. (1980) Transferrinbipyridine iron transfer mediated by hemoproteins, Biochim. Biophys. Acta, 629, 391–398.CrossRefPubMedGoogle Scholar
  63. 63.
    Eguchi, L. A., and Saltman, P. (1987) Kinetics and mechanisms of metal reduction by hemoglobin. 1. Reduction of iron(III) complexes, Inorg. Chem., 26, 3665–3669.CrossRefGoogle Scholar
  64. 64.
    Harrington, J. P., and Hicks, R. L. (1994) Spectral analysis of Fe(III) complex reduction by hemoglobin: possible mechanisms of interaction, Int. J. Biochem., 26, 1111–1117.CrossRefPubMedGoogle Scholar
  65. 65.
    Cassatt, J. C., Marini, C. P., and Bender, J. W. (1975) The reversible reduction of horse metmyoglobin by the iron(II) complex of trans-1,2-diaminocyclohexane-N,N,N′,N′tetraacetate, Biochemistry, 14, 5470–5475.CrossRefPubMedGoogle Scholar
  66. 66.
    Yamada, T., Marini, C. P., and Cassatt, J. C. (1978) Oxidation-reduction reactions of hemoglobin A, hemoglobin M Iwate, and hemoglobin M Hyde Park, Biochemistry, 17, 231–236.CrossRefPubMedGoogle Scholar
  67. 67.
    Lim, A. R., and Mauk, A. G. (1985) Kinetic analysis of metsulphmyoglobin and metmyoglobin reduction by Fe(EDTA)2–, Biochem. J., 229, 765–769.CrossRefPubMedPubMedCentralGoogle Scholar
  68. 68.
    Shekhovtsova, E. A., Goraev, E. V., Sivozhelezov, V. S., and Postnikova, G. B. (2005) The oxidation of sperm whale, horse, and pig oxymyoglobins catalyzed by ferrocyanide ions: kinetics and mechanism, Biophysics (Moscow), 50, 33–42.Google Scholar
  69. 69.
    Shekhovtsova, E. A., Goraev, E. V., Sivozhelezov, V. S., and Postnikova, G. B. (2005) The mechanism of oxymyoglobin oxidation catalyzed by ferrocyanide ions: chemically modified and mutant sperm whale myoglobins, Biophysics (Moscow), 50, 552–561.Google Scholar
  70. 70.
    Postnikova, G. B., Moiseeva, S. A., Goraev, E. V., and Shekhovtsova, E. A. (2007) Ferrocyanide–a novel catalyst for oxymyoglobin oxidation by molecular oxygen, FEBS J., 274, 5360–5369.CrossRefPubMedGoogle Scholar
  71. 71.
    Postnikova, G. B., Tselikova, S. V., and Sivozhelezov, V. S. (1992) Study of electron transport in heme proteins. X. Effect of pH, ionic strength, and zinc ions and the rate of ferricytochrome c reduction by oxymyoglobin from swine heart, Mol. Biol. (Moscow), 26, 880–890.Google Scholar
  72. 72.
    Cher, M., and Davidson, N. (1955) The kinetics of the oxygenation of ferrous iron in phosphoric acid solution, J. Amer. Chem. Soc., 77, 793–798.CrossRefGoogle Scholar
  73. 73.
    Stadtman, E. R., and Oliver, C. N. (1991) Metal-catalyzed oxidation of proteins, J. Biol. Chem., 266, 2005–2008.PubMedGoogle Scholar
  74. 74.
    Gao, X., Liu, Y., and Song, Zh. (2007) Catalytic effect of ferricyanide between myoglobin and luminol and effect of temperature, Luminescence, 22, 88–91.CrossRefPubMedGoogle Scholar
  75. 75.
    Song, Zh., Wang, L., and Hou, S. (2004) A study of the chemiluminescence behavior of myoglobin with luminol and its analytical application, Anal. Bioanal. Chem., 378, 529–535.CrossRefPubMedGoogle Scholar
  76. 76.
    Goucher, C. R., and Taylor, J. F. (1964) Compounds of ferric iron with adenosine triphosphate and other nucleoside phosphates, J. Biol. Chem., 239, 2251–2255.PubMedGoogle Scholar

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Authors and Affiliations

  1. 1.Institute of Cell BiophysicsRussian Academy of SciencesPushchino, Moscow RegionRussia

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