Skip to main content
Log in

Study on the Interaction of Pentachlorophenol with Urease in Aqueous Solution by Multiple Spectroscopic Techniques

  • Published:
Journal of Solution Chemistry Aims and scope Submit manuscript

Abstract

The interactions between pentachlorophenol (PCP) and jack bean urease were studied using UV/vis absorption, CD, fluorescence, synchronous fluorescence, and three-dimensional fluorescence spectroscopic techniques. The fluorescence data showed that the fluorescence quenching of urease by PCP the results of the formation of a PCP–urease complex involving a hydrophobic interaction. The distance r between the donor (urease) and acceptor (PCP) was obtained from the fluorescence resonance energy transfer. The effect of PCP on the conformation of urease was analyzed using UV/vis absorption, synchronous fluorescence and three-dimensional fluorescence spectroscopic techniques. The result showed that PCP can enter into the hydrophobic pocket at the interface of urease and that the micro environments around the tyrosine and tryptophan residues were changed.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  1. Krajewska, B., Ureases, I.: Functional, catalytic and kinetic properties: a review. J. Mol. Catal., B Enzym. 59, 9–21 (2009)

    Article  CAS  Google Scholar 

  2. Krajewska, B., Zaborska, W., Chudy, M.: Multi-step analysis of Hg2+ ion inhibition of jack bean urease. J. Inorg. Biochem. 98, 1160–1168 (2004)

    Article  CAS  Google Scholar 

  3. Jabri, E., Carr, M.B., Hausinger, R.P., Karplus, P.A.: The crystal structure of urease from Klebsiella aerogenes. Science 268, 998–1004 (1995)

    Article  CAS  Google Scholar 

  4. Liu, H.J., Zhan, X.M., Li, K.B., Liu, W.P.: Study on the reaction mechanism of chloroacetanilide herbicides with urease using fluorescence spectrum and high performance liquid chromatography. Spectrosc. Spectr. Anal. 25, 463–466 (2005)

    CAS  Google Scholar 

  5. Zhang, L., Mulrooney, S.B., Leung, A.F.K., Zeng, Y., Ko, B.B.C., Hausinger, R.P., Sun, H.: Inhibition of urease by bismuth(III): Implications for the mechanism of action of bismuth drugs. BioMetals 19, 503–511 (2006)

    Article  CAS  Google Scholar 

  6. Bourguignon, B., Marcenac, F., Keller, H.R., Aguiar, P.F., Massart, D.L.: Simultaneous optimization of pH and organic modifier content of the mobile phase for the separation of chlorophenols using a Doehlert design. J. Chromatogr. 628, 171–189 (1993)

    Article  CAS  Google Scholar 

  7. Carrizo, D., Grimalta, J.O., Ribas-Fito, N., Torrent, M., Sunyer, J.: Pentachlorobenzene, hexachlorobenzene, and pentachlorophenol in children’s serum from industrial and rural populations after restricted use. Ecotoxicol. Environ. Saf. 71, 260–266 (2008)

    Article  CAS  Google Scholar 

  8. Lenke, H., Pieper, D.H., Bruhn, C., Knackmuss, H.J.: Degradation of 2 4-dinitrophenol by two Rhodococcus erythropolis strains, HL 24-1 and HL 24-2. Appl. Environ. Microbiol. 58, 2928–2932 (1992)

    CAS  Google Scholar 

  9. Bukowska, M.: Effects of 2,4-D and its metabolite 2,4-dichlorophenol on antioxidant enzymes and level of glutathione in human erythrocytes. Comp. Biochem. Physiol. 135, 435–441 (2003)

    Article  Google Scholar 

  10. Shen, D.S., Liu, X.W., Feng, H.J.: Effect of easily degradable substrate on anaerobic degradation of pentachlorophenol in an upflow anaerobic sludge blanket (UASB) reactor. J. Hazard. Mater. 119, 239–243 (2005)

    Article  CAS  Google Scholar 

  11. Chang, B.V., Zheng, J.X., Yuan, S.Y.: Effect of alternative electron donors, acceptors and inhibitors on pentachlorophenol dechlorination in soil. Chemosphere 33, 313–320 (1996)

    Article  CAS  Google Scholar 

  12. He, Y., Xu, J.M., Tang, C., Wu, Y.P.: Facilitation of pentachlorophenol degradation in the rhizosphere of ryegrass (Loliu perenne L). Soil. Biol. Biochem. 37, 2017–2024 (2005)

    Article  CAS  Google Scholar 

  13. Lakowicz, J.R.: Principles of Fluorescence Spectroscopy. Plenum Press, New York (1999)

    Google Scholar 

  14. Pham, T.T.P., Oyama, T., Isse, T., Kawamoto, T.: Application of tryptophan fluorescence to assess sensitizing potentials of chemicals. Arch. Environ. Contam. Toxicol. 57, 427–436 (2009)

    Article  CAS  Google Scholar 

  15. Sułkowska, A., Równicka, J., Poźycka, J., Bojko, B., Sułkowski, W.W.: The effect of concentration of guanidine hydrochloride on the sulfasalazine–serum albumin complex. J. Mol. Struct. 744, 775–779 (2005)

    Article  Google Scholar 

  16. Lakowicz, J.R., Weber, G.: Quenching of fluorescence byoxygen: probe for structural fluctuations in macromolecules. Biochemistry 12, 4161–417 (1973)

    Article  CAS  Google Scholar 

  17. Silva, D., Cortez-Moreira, M., Bastos, V.L.F.C., Bastos, J.C., Cortez, C.M.: The interaction of methyl-parathion with serum and albumin of the neo-tropical Piaractus mesopotamicu. Ecotoxicol. Environ. Saf. 73, 32–37 (2010)

    Article  CAS  Google Scholar 

  18. Sharma, A., Schulman, S.G.: Introduction to Fluorescence Spectroscopy. Wiley, New York (1999)

    Google Scholar 

  19. Cao, H., Liu, Q.: Effects of temperature and common ions on binding of puerarin to BSA. J. Solution Chem. 38, 1071–1077 (2009)

    Article  CAS  Google Scholar 

  20. Wang, Y.Q., Zhang, H.M., Zhang, G.C., Tao, W.H., Tang, S.H.: Binding of brucine to human serum albumin. J. Mol. Struct. 830, 840–845 (2007)

    Article  Google Scholar 

  21. Du, W.H., Li, Z.F., Wang, B.H., Zhang, Y.M.: A study on the interaction between cisplatin and urease. Thermochim. Acta 333, 109–114 (1999)

    Article  CAS  Google Scholar 

  22. Tang, B.P., Wang, Y.Q., Zhang, D.Z.: Studies on the interaction between benzidine and the hemocyanin from Chinese mitten crab Eriocheir japonica sinensis. Spectrochim. Acta, Part A, Mol. Biomol. Spectrosc. 73, 676–681 (2009)

    Article  Google Scholar 

  23. Ross, P.D., Subramanian, S.: Thermodynamics of protein association reaction: forces contribution to stability. Biochemistry 20, 3096–3102 (1981)

    Article  CAS  Google Scholar 

  24. Sklar, L.A., Hudson, B.S., Simoni, R.D.: Conjugate polyene fatty acids as fluorescent membrane probes. Biochemistry 16, 5100–5108 (1977)

    Article  CAS  Google Scholar 

  25. Abou-Zied, O.K., Al-Shihi, O.I.K.: Characterization of subdomain IIA binding site of human serum albumin in its native, unfolded, and refolded states using small molecular probes. J. Am. Chem. Soc. 130, 10793–10801 (2008)

    Article  CAS  Google Scholar 

  26. Vial, S., Ghanbajab, J., Forano, C.: Precipitation of Zn2Al LDH by urease enzyme. Chem. Commun. 3, 290–292 (2006)

    Article  Google Scholar 

  27. Zhang, H.M., Wang, Y.Q., Jiang, M.L.: Fluorimetric study of interaction of C. I. Solvent Red 24 with haemoglobin. Dyes Pigm. 82, 156–163 (2009)

    Article  CAS  Google Scholar 

  28. Abert, W.C., Gregory, W.M., Allan, G.S.: The binding interaction of coomassie blue with proteins. Anal. Biochem. 213, 407–413 (1993)

    Article  Google Scholar 

  29. Zhang, Y.Z., Zhou, B., Zhang, X.P., Huang, P., Li, C.H., Liu, Y.: Interaction of malachite green with bovine serum albumin: determination of the binding mechanism and binding site by spectroscopic methods. J. Hazard. Mater. 163, 1345–1352 (2009)

    Article  CAS  Google Scholar 

  30. Cao, S.H., Wang, D.D., Tian, X.Y., Chen, J.W.: Interaction between trans-resveratrol and serum albumin in aqueous solution. J. Solution Chem. 38, 1193–1202 (2009)

    Article  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Yan-Qing Wang.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Wang, YQ., Zhang, GC. & Zhang, HM. Study on the Interaction of Pentachlorophenol with Urease in Aqueous Solution by Multiple Spectroscopic Techniques. J Solution Chem 40, 458–469 (2011). https://doi.org/10.1007/s10953-011-9664-8

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s10953-011-9664-8

Keywords

Navigation