Molecular and Cellular Biochemistry

, Volume 236, Issue 1–2, pp 95–105 | Cite as

Peroxo-bridged divanadate as selective bromide oxidant in bromoperoxidation

  • Swapnalee Sarmah
  • Pankaj Hazarika
  • Nashreen S. Islam


Diperoxovanadate is effective only in presence of free vanadate in vanadium-dependent bromoperoxidation at physiological pH. Peroxide in the form of bridged divanadate complex (VOOV-type), but not the bidentate form as in diperoxovanadate, is proposed to be the oxidant of bromide. In order to obtain direct evidence, peroxo-divanadate complexes with glycyl-glycine, glycyl-alanine and glycyl-asparagine as heteroligands were synthesized. By elemental analysis and spectral studies they were characterized to be triperoxo-divanadates, [V2O2(O2)3(peptide)3].H2O, with the two vanadium atoms bridged by a peroxide and a heteroligand. The dipeptide seems to stabilize the peroxo-bridge by inter-ligand interaction, possibly hydrogen bonding. This is indicated by rapid degradation of these compounds on dissolving in water with partial loss of peroxide accompanied by release of bubbles of oxygen. The 51V-NMR spectra of such solutions showed diperoxovanadate and decavanadate (oligomerized from vanadate) as the products. Additional oxygen was released on treating these solutions with catalase as expected of residual diperoxovanadate. The solid compounds when added to the reaction mixtures showed transient, rapid bromoperoxidation reaction, but not oxidation of NADH or inactivation of glucose oxidase, the other two activities shown by a mixture of diperoxovanadate and vanadyl. This demonstration of peroxide-bridged divanadate as a powerful, selective oxidant of bromide, active at physiological pH, should make it a possible candidate of mimic in the action of vanadium in bromoperoxidase proteins.

bromoperoxidation bromide oxidant peroxo-bridged divanadate diperoxovanadate 


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  1. 1.
    de Boer E, van Kooyk Y, Tromp MGM, Wever R: Bromoperoxidase from Ascophyllum nodosum: A novel class of enzymes containing vanadium as a prosthetic group. Biochim Biophys Acta 869: 48–53, 1986Google Scholar
  2. 2.
    Vitler H, Rehder D: 51V NMR investigation of a vanadate (V)-dependent peroxidase from Ascophyllum nodosum (L) Le. J Inorg Chim Acta 136: L7–L10, 1987Google Scholar
  3. 3.
    Sakurai H, Tsuchiya K: A biomimetic model for vanadium-containing bromoperoxidase. FEBS Lett 260: 109–112, 1990Google Scholar
  4. 4.
    de la Rosa RI, Clague MJ, Butler A: A functional mimic of vanadium bromoperoxidase. J Am Chem Soc 114: 760–761, 1992Google Scholar
  5. 5.
    Bhattacharjee M: Activation of bromide by vanadium pentoxide for the bromination of aromatic hydrocarbons: Reaction mimic for the enzyme bromoperoxidase. Polyhedron 11: 2817–2818, 1992Google Scholar
  6. 6.
    Brooks H, Sicilio F: Electron spin resonance kinetic studies of the oxidation of vanadyl(IV) by hydrogen peroxide. Inorg Chem 10: 2530–2534, 1971Google Scholar
  7. 7.
    Howarth OW, Hunt JR: Peroxo complexes of vanadium(V): A vanadium-51 nuclear magnetic resonance study. J Chem Soc Dalton Trans 1388–1391, 1979Google Scholar
  8. 8.
    Jaswal JS, Tracey AS: Formation and decomposition of peroxovanadium(V) complexes in aqueous solution. Inorg Chem 30: 3718–3722, 1991Google Scholar
  9. 9.
    Ravishankar HN, Ramasarma T: Multiple reactions in oxidation of vanadyl by H2O2. Mol Cell Biochem 129: 9–29, 1993PubMedGoogle Scholar
  10. 10.
    Soedjak HS, Walker JV, Butler A: Inhibition and inactivation of vanadium bromoperoxidase by the substrate hydrogen peroxide and further mechanistic studies. Biochemistry 34: 12689–12696, 1995PubMedGoogle Scholar
  11. 11.
    Bhattacharjee M, Ganguly S, Mukherjee J: Bromination mediated by a vanadium(V)-peroxo complex [V2O2(O2)3(Gly H)2(H2O)2](Gly H = Glycine): A functional model of the enzyme bromoperoxidase. J Chem Res (S): 80–81, 1995Google Scholar
  12. 12.
    Clauge MJ, Butler A: On the mechanism of cis-dioxovanadium(V)-catalyzed oxidation of bromide by hydrogen peroxide: Evidence for a reactive, binuclear vanadium(V) peroxo complex. J Am Chem Soc 117: 3475–3484, 1995Google Scholar
  13. 13.
    Aparna Rao VS, Ravishankar HN, Ramasarma T: Vanadium catalysis in bromoperoxidation reaction. Arch Biochem Biophys 334: 121–134, 1996PubMedGoogle Scholar
  14. 14.
    Ravishankar HN, Ramasarma T: Requirement of a diperoxovanadatederived intermediate for the inter-dependent oxidation of vanadyl and NADH. Arch Biochem Biophys 316: 319–326, 1995PubMedGoogle Scholar
  15. 15.
    Aparna Rao VS, Sima PD, Kanofsky JR, Ramasarma T: Inactivation of glucose oxidase by diperoxovanadate-derived oxidants. Arch Biochem Biophys 369: 163–173, 1999PubMedGoogle Scholar
  16. 16.
    Ravishankar HN, Chaudhuri MK, Ramasarma T: Oxygen-exchange reactions accompanying oxidation of vanadyl sulfate by diperoxovanadate. Inorg Chem 33: 3788–3793, 1994Google Scholar
  17. 17.
    Bhattacharjee M, Chaudhuri MK, Islam NS, Paul PC: Synthesis, characterization and physicochemical properties of peroxo-vanadium(V) complexes with glycine as the hetero-ligand. Inorg Chim Acta 169: 97–100, 1990Google Scholar
  18. 18.
    Sarmah S, Islam NS: A dinuclear peroxo-vanadium(V) complex with coordinated tripeptide. Synthesis, spectra and reactivity in bromoperoxidation. J Chem Res (S): 172–174, 2001Google Scholar
  19. 19.
    Aparna Rao VS, Islam NS, Ramasarma T: Reactivity of µ-peroxobridged dimeric vanadate in bromoperoxidation. Arch Biochem Biophys 342: 289–297, 1997PubMedGoogle Scholar
  20. 20.
    Nolan KB, Soudi AA, Hay RW: Amino acids, peptides and proteins. Roy Soc Chem UK 27: 282–332, 1996Google Scholar
  21. 21.
    Steele MC, Hall FM: Potentiometric determination of titanium and vanadium. Anal Chem Acta 9: 384–388, 1953Google Scholar
  22. 22.
    Chaudhuri MK, Ghosh SK, Islam NS: First synthesis and assessment of alkali-metal triperoxo-vanadate. Inorg Chem 24: 2706–2707, 1985Google Scholar
  23. 23.
    de Boer E, Plat H, Tromp MGM, Weaver R, Franssen MCR, van der Plas HC, Meijer HC, Schoemaker HE: Vanadium containing bromoperoxidase: An example of oxidoreductase with high operational stability in aqueous and organic media. Biotech Bioeng 30: 607–610, 1987Google Scholar
  24. 24.
    Campbell NJ, Dengel AC, Griffith WP: Studies on transition metal preoxo complexes-X. The nature of peroxovanadates in aqueous solution. Polyhedron 8: 1379–1386, 1989Google Scholar
  25. 25.
    Nakamoto K (ed).: Infrared and Raman Spectra of Inorganic and Coordination Compounds. Part B, 5th edn. J Wiley & Sons, New York, 1997, pp 60, 71Google Scholar
  26. 26.
    Miyazawa T, Blout ER: The infrared spectra of polypeptides in various conformations: amide I and amide II bands: J Am Chem Soc 83: 712–716, 1961Google Scholar
  27. 27.
    Meyers RA (ed).: Encyclopedia of Analytical Chemistry. Vol. 2. J Wiley & Sons, New York, 2000, pp 546–559Google Scholar
  28. 28.
    Ravishankar HN, Aparna Rao VS, Ramasarma T: Catalase degrades diperoxovanadate and releases oxygen. Arch Biochem Biophys 321: 477–484, 1995CrossRefPubMedGoogle Scholar
  29. 29.
    Harrison AT, Howarth OW: High-field vanadium-51 and oxygen-17 nuclear magnetic study of peroxovanadates(V). J Chem Soc Dalton Trans 1173–1177, 1985Google Scholar
  30. 30.
    Tracey AS, Jaswal JS: An NMR investigation of the interactions occurring between peroxovanadates and peptides. J Am Chem Soc 114: 3835–3840, 1992Google Scholar
  31. 31.
    Tracey AS, Jaswal JS: Reactions of peroxovanadates with amino acids and related compounds in aqueous solution. Inorg Chem 32: 4235–4243, 1993Google Scholar
  32. 32.
    Einstein FWBE, Batchelor RJ, Angus-Dunne SJ, Tracey AS: A product formed from glycylglycine in presence of vanadate and hydrogen peroxide: the (glycyl-N-hydroglycinato-κ3 N 2 N N,O1) oxoperoxovanadate(V) anion. Inorg Chem 35: 1680–1684, 1996PubMedGoogle Scholar
  33. 33.
    Djordjevic C, Lee M, Sinn E: Oxoperoxo(citrato)-and dioxo(citrato)-vanadates(V): Synthesis, spectra, and structure of a hydroxyl oxygen bridged dimer, K2[VO(O2)(C6H6O7)]2.2H2O. Inorg Chem 28: 719–722 1989Google Scholar
  34. 34.
    Demartin F, Biagioli M, Strinna-Erre L, Panzanelli A, Micera G: Molecular structure of a monoperoxo vanadium(V) complex formed by D,L-lactic acid. Inorg Chim Acta 299: 123–127, 2000Google Scholar
  35. 35.
    Lapstin AE, Smolin YI, Shepeler YF: Structure of tripotassium-fluoroperoxo-bis (fluoroperoxovanadate)(3–) hydrogen fluoride dihydrate. Acta Cryst C46: 1753–1755, 1990Google Scholar
  36. 36.
    Costa Pesoa J, Luz SM, Gillard RD: Oxyvanadium(IV) complexes of peptides with non-coordinating side chains and related ligands; a spectroscopic study. J Chem Soc Dalton Trans 569–576, 1997Google Scholar
  37. 37.
    Hamstra BJ, Colpas GJ, Pecoraro VL: Reactivity of dioxovanadium(V) complexes with hydrogen peroxide: Implications of vanadium haloperoxidase. Inorg Chem 37: 945–955, 1998Google Scholar
  38. 38.
    Casny M, Rehder D, Schmidt H, Vilter H, Conte V: A 17O NMR study of peroxide binding to the active centre of bromoperoxidase from Ascophyllum nidosum. J Inorg Chem 80: 157–160, 2000Google Scholar
  39. 39.
    Rehder D, Holst H, Priebsch W, Vilter H: Vanadate-dependent bromo/iodoperoxidase from Ascophyllum nidosum also contains unspecific low affinity binding sites for vanadate(V): A 51V NMR investigation, including the model peptides phe-glu and gly-tyr. J Inorg Biochem 41: 171–185, 1991Google Scholar
  40. 40.
    Goddard JB, Gonas AM: Kinetics of dissociation of decavanadate ion in basic solutions. Inorg Chem 13: 574–579, 1973Google Scholar
  41. 41.
    Bino A, Cohen S, Hiefuer-Wirguin C: Molecular structure of mixedvalence isopolyvanadate. Inorg Chem 21: 429–431, 1982Google Scholar
  42. 42.
    Messerscmidt A, Prade L, Wever R: Implications for the catalytic mechansim of the vanadium-containing enzyme chloroperoxidase from fungus Curvularia inequalis by X-ray structure of the native and peroxide form. Biol Chem 378: 309–315, 1997PubMedGoogle Scholar
  43. 43.
    Weyand M, Hecht H, Kiess M, Liaud M, Vitler H, Schomburg D. Xray structure determination of a vanadium-dependent haloperoxidase from Ascophyllum nidosum at 2.0 Å resolution. J Mol Biol 293: 595–611, 1999PubMedGoogle Scholar
  44. 44.
    Isupov MN, Dalby AR, Brindley AA, Izumi Y, Tanabe T, Murshudov GN, Littlechild JA: Crystal structure of dodecameric vanadium-dependent bromoperoxidase from red algae Corallina officinalis. J Mol Biol 299: 1035–1049, 2000PubMedGoogle Scholar
  45. 45.
    Hemrika W, Renirie K, Dekker HL, Barnet P, Wever R: From phosphatases to vanadium peroxidases: A similar architecture of the active site. Proc Natl Acad Sci USA 94: 2145–2149, 1997PubMedGoogle Scholar

Copyright information

© Kluwer Academic Publishers 2002

Authors and Affiliations

  • Swapnalee Sarmah
    • 1
  • Pankaj Hazarika
    • 1
  • Nashreen S. Islam
    • 1
  1. 1.Department of Chemical SciencesTezpur UniversityTezpurIndia

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