Mononuclear and dinuclear monoperoxovanadium(V) complexes with a hetero ligand. 1. Self-decomposition reaction, detection of reactive oxygen species, and oxidizing ability

Inorganic Chemistry

Volumn 43, Issue 22, 2004, Pages 7127-7140

  Kanamori, Kan ^a   Nishida, Kazuya ^a   Miyata, Nanako ^a   Shimoyama, Toshiyuki ^a   Hata, Kaori ^a   Mihara, Chie ^a   Okamoto, Ken Ichi ^b   Abe, Yuriko ^c   Hayakawa, Shingo ^d   Matsugo, Seiichi ^d  

^a UNIVERSITY OF TOYAMA   (Japan)

^b UNIVERSITY OF TSUKUBA   (Japan)

^c NARA WOMEN'S UNIVERSITY   (Japan)

^d UNIVERSITY OF YAMANASHI   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

2 OXO 1,3 DIAMINOPROPANE; BOVINE SERUM ALBUMIN; CARBONYL DERIVATIVE; HISTAMINE DERIVATIVE; HISTAMINE N,N DIACETATE; LIGAND; N CARBOXYMETHYLHISTIDINATE; PEROXOVANADIUM; PROPANE; RADICAL; REACTIVE OXYGEN METABOLITE; SODIUM 4 [3 (IODOPHENYL) 2 (4 NITROPHENYL) 2H 5 TETRAZOLIO] 1,3 BENZENEDISULFONATE; SULFONIC ACID DERIVATIVE; UNCLASSIFIED DRUG; VANADIUM DERIVATIVE;

ARTICLE; CHEMICAL REACTION; CHEMICAL STRUCTURE; COMPLEX FORMATION; DECOMPOSITION; ELECTRON SPIN RESONANCE; METAL BINDING; OXIDATION; PROTON NUCLEAR MAGNETIC RESONANCE; REACTION ANALYSIS; ULTRAVIOLET SPECTROSCOPY;

ANIMALS; CATTLE; CRYSTALLOGRAPHY, X-RAY; CYTOCHROMES C; HISTAMINE; HYDROGEN-ION CONCENTRATION; LIGANDS; MAGNETIC RESONANCE SPECTROSCOPY; MOLECULAR CONFORMATION; MOLECULAR STRUCTURE; ORGANOMETALLIC COMPOUNDS; OXIDATION-REDUCTION; REACTIVE OXYGEN SPECIES; SERUM ALBUMIN, BOVINE; TETRAZOLIUM SALTS; VANADIUM;

EID: 7244234380     PISSN: 00201669     EISSN: None     Source Type: Journal    
DOI: 10.1021/ic030292f     Document Type: Article

References (47)

1. Part 2: Reactivity and Mechanism of Bromide Oxidation as Function Models Bromoperoxidases. The manuscript will appear elsewhere.
2. (a) Vanadium in Biological Systems; Chasteen, N. D., Ed.; Kluwer Academic Publishers: Dordrecht, The Netherlands, 1990.
3. (b) Metal Ions in Biological Systems: Vanadium and its role in life: Sigel, H., Sigel, A., Eds.; Marcel Dekker: New York. 1995: Vol. 31.
4. (c) Vanadium in the Environment; Nriagu, J. O., Ed.; John Wiley: New York, 1998.
5. (a) Vilter, H. Vanadium-Dependent Haloperoxidase. In Metal Ions in Biological Systems; Vanadium and its role in life; Sigel, H., Sigel, A., Eds.; Marcel Dekker: New York, 1995; Vol. 31.
6. (b) Wever, R.; Hemrica, W. Vanadium in Enzymes. In Vanadium in the Environment; Nriagu, J. O., Ed.; John Wiley: New York, 1998.
7. (c) Render, D.; Santoni, G.; Licini, G. M.; Schuzke, V.; Meier, B. Coord. Chem. Rev. 2003, 237, 53.
8. (a) Butler, A.; Walker, J. V. Chem. Rev. 1993, 93, 1037.
9. (b) Butler, A.; Clague, M. J.; Meister, G. E. Chem. Rev. 1994, 94, 625.
10. Hirao, T. Chem. Rev. 1997, 97, 2797.
11. Bonchio, M.; Conte, V.; Di Furia, F.; Modena, G.; Moro, S.; Edwards, J. O. Inorg. Chem. 1994, 33, 1631.
12. Render, D.; Costa Pesoa, J.; Geraldes, C. F. G. C.; Castro, M. M. C. A.; Kabanos, T.; Kiss, T.; Meier, B.; Micela, G.; Pettersson, L.; Rangel, M.; Salifoglou, A.; Wang, D. J. Biol. Inorg. Chem. 2002, 7, 384.
13. Thompson, K. H.; McNeill, J. H.; Orvig, C. Chem. Rev. 1999, 99, 2561.
14. Kadota, S.; Fantus, I. G.; Deragon, G.; Cuyda, H. J.; Posner, B. I. J. Biol. Chem. 1978, 262, 8252.
15. Fantus, I. G.; Kadota, S.; Deragon, G.; Foster, B.; Posner, B. I. Biochemistry 1989, 28, 8864.
16. Shaver, A.; Ng, J. B.; Hall, D. A.; Lum, B. S.; Posner. B. I. Inorg. Chem. 1993, 32, 3109.
17. Posner, B. I.; Faure, R.; Burgess, J. W.; Bevan, A. P.; Lachance, D.; Z-Sun, G.; Fantus, I. G.; Ng, J. B.; Hall, D. A.; Lum, B. S.; Shaver, A. J. Biol. Chem. 1994, 269, 4596.
18. Kanamori, K.; Nishida, K.; Miyata, N.; Okamoto, K.; Miyoshi, Y.; Tamura, A.; Sakurai, H. J. Inorg. Biochem. 2001, 86, 649.
19. Djordjevic, C.; Vuletic, N.; Renslo, M. L.; Puryear, B. C.; Alimard, R. Mol. Cell. Biochem. 1995, 153, 25.
20. Conte, V.; Di Furia, F.; Moro, S. J. Mol. Catal. A: Chem. 1997, 120, 93.
21. Thompson, R. C. Inorg. Chem. 1983, 22, 584.
22. Mimoun, H.; Saussine, L.; Daire, E.; Postal, M.; Fischer, J.; Weiss, R. J. Am. Chem. Soc. 1983, 105, 3101.
23. (a) Djordjevic, C.; Vuletic, N.; Renslo, M. L.; Puryear, B. C.; Alimard, R. Moll. Cell Biochem. 1985, 153, 25.
24. (b) Djordjevic, C.; Wampler, G. L. J. Inorg. Biochem. 1985, 25, 51.
25. Shi, X.; Dalal, N. S. Arch. Biochem. Biophys. 1993, 307, 336.
26. SIR 92: Altomare, A.; Burla, M. C.; Camalli, M.; Cascarano, M.; Giacovazzo, C.; Guagliardi, A.; Polidori, G. J. Appl. Crystallogr. 1994, 27, 435.
27. TEXAN. Single-Crystal Structure Analysis Software, version 1.10; Molecular Structure Corporation: The Woodlands, TX, 1997.
28. Butler, J.; Jayson, G. G.; Swallow, A. J. Biochim. Biophys. Acta 1975, 488, 215.
29. Since the reduced form of cytochrome c is fairly unstable and the 550-nm band disappeared when the reaction solution allowed to stand for a long period, we limited the measurement time to 15 min.
30. Ukeda, H.; Kawana, D.; Maeda, S.; Sawamura, M. Biosci. Biotechnol. Biochem. 1999, 66, 485.
31. (a) Matsugo, S.; Yan, L. J.; Han, D.; Trischler, H. J.; Packer, L. Biochem. Biophys. Res. Commun. 1995, 208, 161.
32. (b) Ali, M. A.; Yasui, F.; Matsugo, S.; Konishi, T. Free Rad. Res. 2000, 32, 485.
33. Frank, T. Anal. Biochem. 1969, 27, 502.
34. Djordjevic, C.; Lee, M.; Sinn, E. Inorg. Chem. 1989, 28, 719.
35. Demartin, F.; Biagioli, M.; Strinna-Erre, L.; Panzanelli, A.; Micera, G. Inorg. Chim. Acta 2000, 299, 123.
36. Messerschmidt, A.; Prade, L.; Wever, R. Biol. Chem. 1997, 378, 309.
37. Kojima, A.; Okazaki, K.; Ooi, S.; Saito, K. Inorg. Chem. 1983, 22, 1168.
38. Kumagai, H.; Kawata, S.; Kitagawa, S.; Kanamori, K.; Okamoto, K. Chem. Lett. 1997, 249.
39. Nishizawa, M.; Hirotsu, K.; Ooi, S.; Saito, K. J. Chem. Soc., Chem. Commun. 1979, 707.
40. Rehder, D. Inorganic Considerations on the Function of Vanadium in Biological Systems. In Metal Ions in Biological Systems: Vanadium and its role in life: Sigel, H., Sigel, A., Eds.; Marcel Dekker: New York, 1995; Vol. 31.
41. Walker, J. V.; Butler, A. Inorg. Chim. Acta 1996, 243, 201.
42. One reviewer suggested that the difference between Trolox and TBPC is because Trolox has a lower oxidation potential than TBPC and is much more easily oxidized by vanadates. Another suggestion is that the chroman moiety of Trolox with hydrogen peroxide would give several radical side reactions that might be responsible for the observed shortening of the induction period.
43. Kohno, M.; Yamada, M.; Mitsuta, K.; Mizuta, Y.; Yoshikawa, T. Bull. Chem. Soc. Jpn. 1991, 24, 1285.
44. Brooks, H. B.; Sicilio, F. Inorg. Chem. 1971, 10, 2530.
45. Thompson, R. C. Inorg. Chem. 1982, 21, 859.
46. Yasui, F.; Matsugo, S. ITE Lett. 2001, 2, 537.
47. Zhang, Z.; Leonard, S. S.; Huang, C.; Vallyathan V.; Castranova, V.; Shi, X. Free Radical Biol. Med. 2003, 34, 1333.