Startseite The Thermodynamic and pH Metric Binding Studies of Cu+2 Ions with Egg Protein by Spectrometric and Diffusion Current Techniques
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The Thermodynamic and pH Metric Binding Studies of Cu+2 Ions with Egg Protein by Spectrometric and Diffusion Current Techniques

  • Shveta Acharya und Arun Kumar Sharma EMAIL logo
Veröffentlicht/Copyright: 12. Juni 2019

Abstract

Transition metals have unique efficacy in catalyzing various industrial reactions and also in living system, the redox reaction and redox changes in the metal ions catalyzed valence changes in the substrate molecule. The survey of the existing literature revealed that the binding of Molybdenum, Vanadium, Zinc, Cadmium, Copper, Nickel and Cobalt with the protein is well known but no binding studies of copper metal with egg protein are reported. With a view to extend the existing knowledge of ecological nature of metal-protein system, it was thought of interest to investigate the properties of metal-protein mixture. Investigations on the aspects of these binding problems were planned and their bindings constants have been determined using suitable physico-chemical methods. The pH metric, diffusion current measurements, spectrophotometric methods have been used on the binding of copper ions with albumin. The effect of physico-chemical factors on interaction between divalent metal ion i.e. copper with albumin has been discussed. On the basis of observed results, it is found that the binding data were dependent on pH and temperature. From scatchard plots, the intrinsic association constants (k) and the number of binding sites (n) were calculated and found high at lower pH and temperatures. Therefore, a lower temperature and lower pH offered more sites in the protein molecule for interaction with copper (II) ions. The enthalpy (ΔH), entropy (ΔS) changes, free energy change (ΔG°) have been calculated.

Acknowledgments

The authors pay their sincere gratitude to UGC for financial assistance as TRF and Principal, Govt. College Kota and S.P.C. Govt. College Ajmer, Rajasthan (India) for providing necessary research facilities to accomplish this study.

References

1. A. Barth, Prog. Biophys. Mol. Biol. 74 (2000) 141.10.1016/S0079-6107(00)00021-3Suche in Google Scholar

2. T. Hoffmann, L. Dougan, Chem. Soc. Rev. 41 (2012) 4781.10.1039/c2cs35033eSuche in Google Scholar

3. D. C. Harris, Biochemistry 16 (1977) 560.10.1021/bi00622a033Suche in Google Scholar

4. S. Ro, C.-J. Yoon, Z. Phys. Chem. 214 (2000) 1699.10.1524/zpch.2000.214.12.1699Suche in Google Scholar

5. S. Köppen, B. Ohler, W. Langel, Z. Phys. Chem. 221 (2007) 3.10.1524/zpch.2007.221.1.3Suche in Google Scholar

6. J. P. S. Arora, R. P. Singh, S. Soam, R. Sharma, Bioelectrochem. Bioenerg. 10 (1983) 57.10.1016/0302-4598(83)80105-6Suche in Google Scholar

7. J. P. S. Arora, R. P. Singh, S. Soam, S. P. Singh, R. Kumar, Bioelectrochem. Bioererg. 10 (1983) 289.10.1016/0302-4598(83)85087-9Suche in Google Scholar

8. S. Acharya, A. K. Sharma, Curr. Phy. Chem. 8 (2018) 186.10.2174/1877946808666181002102441Suche in Google Scholar

9. M. M. Harding, Acta Crystallor. D. Biol. Crystallogr. 56 (2000) 857.10.1107/S0907444900005849Suche in Google Scholar

10. J. Peisach, W. E. Blumberg, Arch. Biochem. Biophys. 165 (1974) 691.10.1016/0003-9861(74)90298-7Suche in Google Scholar

11. R. Nandi, S. Laskar, B. Saha. Res. Chem. Intermed. 43 (2017) 1619.10.1007/s11164-016-2719-0Suche in Google Scholar

12. M. Kirberger, H. C. Wong, J. Jiang, J. J. Yang, J. Inorg. Biochem. 125 (2013) 40.10.1016/j.jinorgbio.2013.04.002Suche in Google Scholar

13. J. P. S. Arora, R. P. Singh, S. Soam, S. P. Singh, R. Kumar, Bioelectrochem. Bioenerg. 10 (1983) 441.10.1016/0302-4598(83)80071-3Suche in Google Scholar

14. M. Laitaoja, J. Valjakka, Inorg. Chem. 52 (2013) 10983.10.1021/ic401072dSuche in Google Scholar

15. A. K. Sharma, S. Acharya, Z. Phy. Chem. 233 (2018) 691.10.1515/zpch-2018-1181Suche in Google Scholar

16. H. Irving, R. J. P. Williams, J. Chem. Soc. 77 (1955) 1384.10.1021/ja01610a098Suche in Google Scholar

17. E. Breslow, F. R. N. Gurd, J. Biological. Chem. 238 (1968) 1332.10.1016/S0021-9258(18)81184-XSuche in Google Scholar

18. J. P. S. Arora, R. P. Singh, S. Jain, S. P. Singh, A, Kumar, Bioelectiochem. Bio. Enegy 13 (1984) 329.10.1016/0302-4598(84)87035-XSuche in Google Scholar

19. R. Chatterjee, S. P. Mitra, D. K. Chattoraj, Ind. J. Biochem. Biophys. 16 (1979) 22.Suche in Google Scholar

20. S. R. Verma, J. P. S. Arora, J. S. Shankar, R. Chand, Water Air Soil Pollut. 36 (1987) 247.10.1007/BF00229671Suche in Google Scholar

21. S. Acharya, A. K. Sharma, Binding studies of metal ions and dyes with biopolymers “ISBN 978-613-8-38659-9” LAP LAMBERT Academic Publisher, Germany 2018.Suche in Google Scholar

22. H. Haraguchi, J. Anal. At. Spectrom. 19 (2004) 5.10.1039/b308213jSuche in Google Scholar

23. G. Scatchard, E. S. Black, J. Phys. Chem. 53 (1949) 88.10.1021/j150466a007Suche in Google Scholar

24. S. Acharya, A. K. Sharma, Interaction studies of metals and surfactant with protein “ISBN 978-613-8-38751-0” LAP LAMBERT Academic Publisher Germany (2018).Suche in Google Scholar

25. N. J. Greenfield, Nat. Protoc. 1 (2006) 2876.10.1038/nprot.2006.202Suche in Google Scholar PubMed PubMed Central

26. U. Sakaguchi, A. W. Addison, J. Chem. Soc. Dalton Trans. 0 (1979) 600.10.1039/dt9790000600Suche in Google Scholar

27. J. Szpunar, Anal. Bioanal. Chem. 378 (2004) 54.10.1007/s00216-003-2333-zSuche in Google Scholar PubMed

28. A. Zuorro, R. Lavecchia, Asia-Pacific J. Chem. Eng. 7 (2012) 329.10.1002/apj.1652Suche in Google Scholar

29. E. E. Bernanducci, W. F. Schwindinger, J. L. Hughey, K. Krogh-Jespersen, H. J. Schugar, J. Am. Chem. Soc. 103 (1981) 1686.10.1021/ja00397a017Suche in Google Scholar

30. P. G. Daniele, E. Prenesti, G. Ostacoli, J. Chem. Soc. Dalton. Trans. 0 (1996) 3269.10.1039/DT9960003269Suche in Google Scholar

31. L. Rivillas-Acevedo, R. Grande-Aztatzi, I. Lomel, J. E. Garcıa, E. Barrios, S. Teloxa, A. Vela, L. Quin-tanar, Inorg Chem, 50 (2011) 1956.10.1021/ic102381jSuche in Google Scholar PubMed

32. E. I. Solomon, R. K. Szilagyi, S. DeBeer George, L. Basumallick, Chem. Rev. 104 (2004) 419.10.1021/cr0206317Suche in Google Scholar PubMed

Received: 2018-10-25
Accepted: 2019-05-09
Published Online: 2019-06-12
Published in Print: 2020-03-26

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