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Kinetics of Azide Binding to Chloroperoxidase in Water and Reversed Micelles of Sodium Dodecylsulphate, Hexanol and Water

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Reactions in Compartmentalized Liquids

Abstract

The kinetics of azide binding to chloroperoxidase (ClP) in aqueous solution and reversed micelles of sodium dodecy1sulphate (SDS), hexanol and water has been studied over a wide pH range using the Iodine Laser Temperature Jump (ILTJ) method. The pH dependence of the forward rate constant (kon) in aqueous solution eliminates several possible mechanisms and suggests that the transfer of azide to the enzyme occurs via HN3. The pH dependence of kon in the reversed micellar system suggests there is a change in the environment around the active site of the enzyme, which results in a lowering of both the limiting rate for the reaction (found at low pH’s) and the pH sensed by the enzyme. The kinetic results could be fitted to a model where ClP is located near the surface of the micelle, resulting in both a lowering of the pH around the enzyme (ca. 2 units) and a decrease in the amount of azide able to bind to the enzyme.

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References

  1. Luisi P.L., Giomini M., Pileni, M.P., Robinson B.H. (1988)Biochimica et. Biophysica Acta 947:209

    CAS  Google Scholar 

  2. Luisi P.L., Magid L.J. (1986) Crit. Rev. Biochem. 20:409

    Article  CAS  Google Scholar 

  3. Luisi P. L., Steinmann-Hofmann B. (1987) Methods In Enzymology, Academic Press, London, pp 188–216

    Google Scholar 

  4. Smith R.E., Luisi P.L. (1980) Helv. Chimica Acta 242:2302

    Article  Google Scholar 

  5. Barbaric S., Luisi P.L. (1981) J. Am. Chem. Soc. 103:4239

    Article  CAS  Google Scholar 

  6. Menger F.M., Yamada K. (1979) J. Am. Chem. Soc. 101:22

    Google Scholar 

  7. Franssen M.C.R. (1987) Ph. D. Thesis, Landbouw Univ., Netherlands

    Google Scholar 

  8. Franssen M.C.R., Weijland J.G., Vinchen J.P., Lanne C., Van der Plas HC (1987) btud. Org. Chem. 29:289

    CAS  Google Scholar 

  9. Douzou P., Keh E., Balny C. (1979) Proc. Natl. Acad. Sci. 76:681

    Article  CAS  Google Scholar 

  10. Martinek K., Levanshov A.V., Klyachko N.L.I., Berenzin J.V. (1978) Dolk. Acad. Nauk. SSR Eng. ea. (1978) 236:95.

    Google Scholar 

  11. Levanshov A.V., Khmelnitsky YU.L., Klyachlo N.L., Martinek K. (1984) Surfactants in Solution, Plenum Press, New York

    Google Scholar 

  12. Morishima I., Ogawa S., Xonezawa T., Nakatani H., Hiromi K., Sano T., Yasunaga T. Biochem Biophys. Research Corom. 83:724

    Google Scholar 

  13. Holzwarth J.F., Schmidt A., Wolff H., Volk R. (1977) J. Phys. Chem 81:2300

    Article  CAS  Google Scholar 

  14. Holzwarth J.F. (1979) Techniques and Applications of Fast Reactions In Solution, Gettins W.J. and wyn- ones E. eds., D. Reidel publshing co., Dordrecht, Holland, pp 47–70

    Google Scholar 

  15. Banntster J.J., Gormally J., King T.A., Holzwarth J.F. (1984) Chem. Britian 20:227

    Google Scholar 

  16. Holzwarth J.F., Meyer F., Pickard M., Dunford H.B. (1988) Biochemistry 27:6628

    Article  CAS  Google Scholar 

  17. Carmicheal R.D., Jones A., Pickard M.A. (1986) Appl. Environmental Microbiol. 51:276

    Google Scholar 

  18. Glasoe P.K., Long F.A. (1960) J. Phys. Chem. 64:188

    Article  CAS  Google Scholar 

  19. Rubin B. I., Van Middlesworth J., Thomas K., Hager L. (1982) Biological Chem. 257:7768

    CAS  Google Scholar 

  20. Reinsborough V.C., Holzwarth J.F. (1986) Can. J. Chem. 64:955

    Article  CAS  Google Scholar 

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© 1989 Springer-Verlag Berlin Heidelberg

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Jobe, D.J., Dunford, H.B., Pickard, M., Holzwarth, J.F. (1989). Kinetics of Azide Binding to Chloroperoxidase in Water and Reversed Micelles of Sodium Dodecylsulphate, Hexanol and Water. In: Knoche, W., Schomäcker, R. (eds) Reactions in Compartmentalized Liquids. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-74787-8_5

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  • DOI: https://doi.org/10.1007/978-3-642-74787-8_5

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-540-51188-5

  • Online ISBN: 978-3-642-74787-8

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