The mechanism of azide activation of polyphenol oxidase II from tobacco

• Autorzy: Shi C. , Liu Q. , Dai Y. , Xie Y. , Xu X.
• Języki publikacji: EN

Abstrakty

EN

So far, azide has been consistently reported to act as an inhibitor of metal enzymes, especially copper proteins. The present work shows that azide can also act as an acti­vator of polyphenol oxidase II (PPO II) from tobacco leaves. From the square-wave voltammetry of native PPO II, peroxide-PPO II complex and azide-PPO II complex, the reduction of nitro blue tetrazolium by the enzymes and activation of PPO II by peroxide it follows that the binding of azide to PPO II induces the formation of CuO2 2-Cu in the active site of PPO II from CuO2 -Cu in native PPO II. The reason for azide acting as an activator can be attributed to azide complexing with PPO II, thus inducing the formation of CuO2 2-Cu, which is the active site of the peroxide-PPO II complex in which peroxide plays the role of activator.

Słowa kluczowe

EN

peroxide activation; azide activation; superoxide activation; polyphenoloxidase; metal enzyme; polyphenol oxidase; copper protein; tobacco; leaf

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2002
• Tom: 49
• Numer: 4
• Opis fizyczny: p.1029-1035,fig.

Twórcy

autor

Shi C.

• University of Sciences and Technology of China, Hefei, 230026, P.R.China

autor

Liu Q.

autor

Dai Y.

autor

Xie Y.

autor

Xu X.

Bibliografia

• Ai JY, Broadwater JA, Loehr TM, Sandersloehr J, Fox BG. (1997) Peroxodiferric intermediate of stearoyl-acyl carrier protein Delta desaturase: oxidase reactivity during single turnover and implications for the mechanism of desaturation. J Biol Inorg Chem.; 2: 37-45.
• Bradford MM. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem.; 72: 248-54.
• Brookes BA, Ball JC, Compton RG. (1999) Simulation of square wave voltammetry: reversible electrode processes. J Phys Chem B.; 103: 5289-98.
• Cole JL, Clark PA, Solomon EI. (1990) Spectroscopic and chemical studies of the laccase trinuclear copper active site: geometric and electronic structure. J Am Chem Soc.; 112: 9534-48.
• Eichen C, Krebs B, Saccbettini JC. (1999) Catechol oxidase-structure and activity. Curr Opin Struct Biol.; 9: 677-83.
• Gromov I, Marchesiui A, Farver OI, Pecht I, Goldfarb D. (1999) Azide binding to the trinuclear copper center in laccase and ascorbate oxidase. Eur J Biochem.; 266: 820-30.
• Jewett SL, Olmsted HK, Marach JA, Rojas F, Silva K. (2000) Anion protection of CuZnSOD during peroxidative activity with H2O2. Biochem Biophys Res Commun..; 274: 57-60.
• Li WB, Palmer G. (1993) Spectroscopic characterization of the interaction of azide and thiocyanate with the binuclear center of cytochrome-oxidase — evidence for multiple ligand sites. Biochemistry.; 32: 1833-43.
• Little RH, Cheesman MR, Thomson AJ, Greenwood C, Watmough NJ. (1996) Cytochrome bo from Escherichia coli: binding of azide to Cu-B. Biochemistry.; 35: 13780-7.
• Malmstrom BG, Andreasson LE, Reinhammar B. (1975) In Enzymes. Boyer PD. ed. 12: 507-79. Academic Press, NY.
• Palmieri G, Giardina P, Bianco C, Scaloni A, Sannia G. (1997) A novel white laccase from Pleurotus ostreatus. J Biol Chem.; 272: 31301-7.
• Pate JE, Ross PK, Thamann TJ, Reed CA, Karlin KD, Thomas SN, Solomon EI. (1989) Spectroscopic studies of the charge transfer and vibrational features of binuclear copper(ii) azide complexes: comparison to the coupled binuclear copper active site in Met azide hemocyanin and tyrosinase. J Am Chem Soc.; 111: 5198-209.
• Robb DA. (1984) In Cop per proteins and copper enzymes. Lontie R. ed, 2, 207-41. CRC Press, Boca Raton, FL.
• Rompel A, Fischer H, Meiwes D, Buldt- Karentzopoulos K, Dillinger R, Tuczek F, Witzel H, Krebs B. (1999) Purification and spectroscopic studies on catechol oxidases from Lycopus europaeus and Populus nigra: evidence for a dinuclear copper center of type 3 and spectroscopic similarities to tyrosinase and hemocyanin. J Biol Inorg Chem.; 4: 56-63.
• Schwartz B, Olgin AK, Klinman JP. (2001) The role of copper in topa quinone biogenesis and catalysis, as probed by azide inhibition of a copper amine oxidase from yeast. Biochemistry.; 40: 2954-63.
• Sheline R, Strothkamp KG. (1980) The pH dependence of the inhibition of ascorbate oxidase by anions. Biochem Biophys Res Commun.; 96: 1343-8.
• Shi C, Dai Y, Xia B, Xu X, Xie Y, Liu Q. (2001a) The purification and spectral properties of polyphenol oxidase I from Nicotiana t abacum. Plant Mol Biol Rep.; 19: 381-2.
• Shi C, Dai Y, Xu X, Xie Y, Liu Q. (2001b) UV/VIS spectra studies on the polyphenol oxidase II. (PPO II) from tobacco. Spectroscopy Lett.; 34: 675-83.
• Shi C, Dai Y, Xu X, Xie Y, Han H, Liu Q. (2001c) Interaction between azide and PPO II from tobacco. J Protein Chem.; 20: 463-8.
• Shi C, Dai Y, Xu X, Xie Y, Liu Q. (2002) The purification of polyphenol oxidase from tobacco. Protein Expr Purif.; 24: 51-5.
• Solomon EI, Sundaram UM, Mochonkin TE. (1996) Multicopper oxidase and oxygenases. Chem Rev.; 96: 2563-605.
• Tavagnacco C, Moszner M, Cozzi S, Peressinin S, Costa G. (1998) Electrocatalytic dioxygen reduction in the presence of a rhodoxime. JElectroanalyt Chem.; 448: 41-50.
• Vamvouka M, Muller W, Ludwig B, Varotsis C. (1999) Fourier transform infrared and resonance Raman studies of the interaction of azide with cytochrome c oxidase from Paracoccus denitrificans. JPhys Chem B.; 103: 3030-4.
• Varotsis C, Vamvouka M. (1999) Resonance Raman and Fourier transform infrared detection of azide binding to the binuclear center of cytochrome bo(3) oxidase from Escherichia co li. J Phys Chem B.; 103: 3942-6.