A discrepancy in superoxide scavenging activity between the ESR-Spin trapping method and the luminol chemiluminescence method

Bioscience, Biotechnology and Biochemistry

Volumn 71, Issue 6, 2007, Pages 1505-1513

  Sato, Emiko ^a   Niwano, Yoshimi ^a,b   Mokudai, Takayuki ^a   Kohno, Masahiro ^a   Matsuyama, Yukihiko ^c   Kim, Daekyung ^b,d,e   Oda, Tatsuya ^e  

^a TOHOKU UNIVERSITY   (Japan)

^b Sunny Health Holdings Co Ltd   (Japan)

^c FISHERIES RESEARCH AGENCY   (Japan)

^d Jeju National University   (South Korea)

^e NAGASAKI UNIVERSITY   (Japan)

Author keywords

Electron spin resonance (ESR) spin trapping method; Horseradish peroxidase (HRP); Luminol chemiluminescence method; Superoxide scavenging activity

Indexed keywords

CHEMILUMINESCENCE; COMPLEXATION; PARAMAGNETIC RESONANCE; REACTION KINETICS; SCAVENGING;

ESR-SPIN TRAPPING METHOD; FERRIC-PROTEIN COMPLEXES; LUMINOL CHEMILUMINESCENCE METHOD; SIGNAL INTENSITY; SUPEROXIDE SCAVENGING ACTIVITY;

BIOCHEMISTRY;

IRON BINDING PROTEIN; LUMINOL; SCAVENGER; SUPEROXIDE;

ARTICLE; CHEMOLUMINESCENCE; COMPARATIVE STUDY; ELECTRON SPIN RESONANCE; METABOLISM; METHODOLOGY; REPRODUCIBILITY; SPIN LABELING; STANDARD; TECHNIQUE;

CHEMILUMINESCENT MEASUREMENTS; ELECTRON SPIN RESONANCE SPECTROSCOPY; FREE RADICAL SCAVENGERS; IRON-BINDING PROTEINS; LUMINOL; METHODS; REPRODUCIBILITY OF RESULTS; SPIN LABELS; SUPEROXIDES;

ALEXANDRIUM AFFINE; ARMORACIA RUSTICANA; CHATTONELLA OVATA; DINOPHYCEAE; GYMNODINIUM; MASTIGOPHORA (FLAGELLATES); RAPHIDOPHYCEAE;

EID: 34347371302     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.70011     Document Type: Article

References (39)

1. Hallegraeff, G. M., A review of harmful algal blooms and their apparent global increase. Phycologia, 32, 7999 (1993).
2. Honjo, T., The biology and prediction of representative red tides associated with fish kills in Japan. Rev. Fish. Sci., 2, 225253 (1994).
3. Shimada, M., Kawamoto, Y., Nakatsuka, Y., and Watanabe, M., Localization of superoxide anion in the red tide alga Chattonella antiqua. J. Histchem. Cytochem., 41, 507-511 (1993).
4. Tanaka, K., Muto, Y., and Shimada, M., Generation of superoxide anion radicals by the marine phytoplankton organism, Chattonella antiqua. J. Plankton Res., 16, 161-169 (1994).
5. Tanaka, K., Yoshimatsu, S., and Shimada, M., Generation of superoxide anions by Chattonella antiqua: possible causes for fish death by 'Red Tide.' Experientia, 48, 888-890 (1992).
6. Oda, T., Ishimatsu, A., Shimada, M., Takeshita, S., and Muramatsu, T., Oxygen-radical-mediated toxic effects of the red tide flagellate Chattonella marina on Vibrio alginolyticus. Mar. Biol., 112, 505-509 (1992).
7. Oda, T., Ishimatsu, A., Takeshita, S., and Muramatsu, T., Hydrogen peroxide production by the red-tide flagellate Chattonella marina. Biosci. Biotechnol. Biochem., 58, 455-458 (1994).
8. Oda, T., Akaike, T., Sato, K., Ishimatsu, A., Takeshita, S., Muramatsu, T., and Maeda, H., Hydroxyl radical generation by red tide algae. Arch. Biochem. Biophys., 294, 38-43 (1992).
9. Oda, T., Nakamura, A., Shikayama, M., Kawano, I., Ishimatsu, A., and Muramatsu, T., Generation of reactive oxygen species by raphidophycean phytoplankton. Biosci. Biotechnol. Biochem., 61, 1658-1662 (1997).
10. Fridovich, I., Biological effects of the superoxide radical. Arch. Biochem. Biophys., 247, 1-11 (1986).
11. Miller, D. M., Buettner, G. R., and Aust, S. D., Transition metals as catalysts of "autoxidation" reactions. Free Radic. Biol. Med., 8, 95-108 (1990).
12. Slater, T. F., Free-radical mechanisms in tissue injury. Biochem. J., 222, 1-15 (1984).
13. Halliwell, B., and Gutteridge, J. M., Oxygen toxicity, oxygen radicals, transition metals and disease. Biochem. J., 219, 1-14 (1984).
14. Oda, T., Akaike, T., Hamamoto, T., Suzuki, F., Hirano, T., and Maeda, H., Oxygen radicals in influenza-induced pathogenesis and treatment with pyran polymer conjugated SOD. Science, 244, 974-976 (1989).
15. Hiroishi, S., Okada, H., Imai, I., and Yoshida, T., High toxicity of the novel bloom-forming species Chattonella ovata (Raphidophyceae) to cultured fish. Harmful Algae, 4, 783-787 (2005).
16. Yang, C. Z., Albright, L. J., and Yousif, A. N., Oxygen-radical-mediated effects of the toxic phytoplankter Heterosigma carterae on juvenile rainbow trout Oncorhynchus mykiss. Dis. Aquat. Org., 23, 101-108 (1995).
17. Kim, D., Oda, T., and Muramatsu, T., Radical scavengers in red tide plankton, Chattonella marina. Bull. Fac. Fish. Nagasaki Univ. (in Japanese), 82, 93-97 (2001).
18. Sato, E., Niwano, Y., Matsuyama, Y., Kim, D., Nakashima, T., Oda, T., and Kohno, M., Some dinophycean red tide plankton species generate a superoxide scavenging substance. Biosci. Biotechnol. Biochem., 71, 704-710 (2007).
19. Niwano, Y., Sato, E., Kohno, M., Matsuyama, Y., Kim, D., and Oda, T., Antioxidant properties of aqueous extracts from red tide plankton cultures. Biosci. Biotechnol. Biochem., 71, 1145-1153 (2007).
20. Nakamura, M., and Nakamura, S., One- and two-electron oxidations of luminol by peroxidase systems. Free Radic. Biol. Med., 24, 537-544 (1998).
21. Dodeigne, C., Thunus, L., and Lejeune, R., Chemiluminescence as diagnostic tool: a review. Talanta, 51, 415-439 (2000).
22. Fridovich, I., Quantitative aspects of the production of superoxide anion radical by milk xanthine oxidase. J. Biol. Chem., 245, 4053-4057 (1970).
23. - in the chemiluminescence of luminol. Photochemist. Photobiol., 18, 451-455 (1973).
24. Kabuto, H., Nishizawa, M., Tada, M., Higashio, C., Shishibori, T., and Kohno, M., Zingerone [4-(4-hydroxy-3-methoxyphenyl)-2-butanone] prevents 6-hydroxydopamine-induced dopamine depression in mouse striatum and increases superoxide scavenging activity in serum. Neurochem. Res., 30, 325-332 (2005).
25. Sato, E., Kohno, M., Hamano, H., and Niwano, Y., Increased anti-oxidative potency of garlic by spontaneous short-term fermentation. Plant Foods Hum. Nutri., 61, 157-160 (2006).
26. Imada, I., Sato, E. F., Miyamoto, M., Ichimori, Y., Minamiyama, Y., Konaka, R., and Inoue, M., Analysis of reactive oxygen species generated by neutrophils using a chemiluminescence probe L-012. Anal. Biochem., 271, 53-58 (1999).
27. Todoki, K., Lee, C., Miyazaki, H., and Oomori, Y., Characteristics of interaction between luminol chemiluminescence and a metal component enzyme (secondary report). Jikikyoumei to Igaku (in Japnese), 12, 65-67 (2001).
28. Maltempo, M. M., The spin 3/2 state and quantum spin mixtures in haem proteins. Q. Rev. Biophys., 9, 181-215 (1976).
29. Harris, G., Spin-mixed states of ferric ion in complexes of tetragonal symmetry. Theor. Chim. Acta (Berlin), 10, 119-154 (1968).
30. 2O and OH-ligand field strength on the magnetochemical series relative to the spectrochemical series: novel 1-equiv water chemistry of iron (III) tetraporphyrin complexes. J. Am. Chem. Soc., 122, 4460-4467 (2000).
31. Boersma, A. D., and Goff, H. M., Multinuclear magnetic resonance spectrometry of spin-admixed S = 3/2, 5/2 iron (III) porohyrins. Inorg. Chem., 21, 581-586 (1982).
32. Reyes-Ortega, Y., Álvarez-Toledano, C., Ramirez-Rosales, D., Sánchez-Sandoval, A., González-Vergara, E., and Zamorano-Ulloa, R., Pinch-porphyrins, new spectroscopic and kinetic models of peroxidases. J. Chem. Soc., Dalton Trans., 667-674 (1998).
33. Walker, F. A., Proton NMR and EPR spectroscopy of paramagnetic metallopoiphyrins. In "The Porphyrins Handbook," eds. Kadish, K. M., Smith, K. M., and Guilard, R., Academic Press, San Diego, pp. 81-175 (1999).
34. Reed, J. C. A., Mashiko, T., Bentley, S. P., Kastner, M. E., Scheidt, W. R., Spartalian, K., and Lang, G., The missing heme spin state and a model for cytochrome c′. The mixed S = 3/2, 5/2 intermediate spin ferric porphyrin: perchlorato (meso-tetraphenylporphynato) iron (III). J. Am. Chem. Soc., 101, 2948-2958 (1979).
35. Gismelseed, A., Bominaar, E. L., Bill, E., Trautwein, A. X., Winkler, H., Nasri, H., Doppelt, P., Mandon, D., Fischer, J., and Weiss, R., Six-coordinate quantum-mechanically weakly spin-mixed (S = 3/2, 5/2) (triflato)aquioiron (III) "picket-fence" porphyrin complex: synthesis and structural, Mössbauer, EPR, and magnetic characterization. Inorg. Chem., 29, 2741-2749 (1990).
36. 4. Inorg. Chem., 28, 1591-1595 (1989).
37. Puppo, A., and Halliwell, B., Formation of hydroxyl radicals from hydrogen peroxide in the presence of iron. Is haemoglobin a biological Fenton reagent? Biochem. J., 249, 185-190 (1988).
38. Pecci, L., Montefoschi, G., and Cavallini, D., Some new details of the copper-hydrogen peroxide interaction. Biochem. Biophys. Res. Commum., 235, 264-267 (1997).
39. 2 plus Cu, Zn-superoxide dismutase reflects the activity of free copper released from the oxidatively damaged enzyme. J. Biol. Chem., 267, 25371-25377 (1992).