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Cyanobacteria Spirulina Platensis Basic Protein C-Phycocyanin and Zn(II) Ions

Received: 21 July 2016    Accepted: 25 July 2016    Published: 14 September 2016
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Abstract

The interaction of Zn(II) ions with cyanobacteria Spirulina platensis basic protein C-phycocyanin (C-PC) is studied by fluorescence spectroscopy.Stern–Volmer quenching constant value for Zn(II)–C-PC is determined. The binding energy of Zn(II) ions with C-phycocyanin is determined using equilibrium dialysis and atomic absorption spectroscopy. Cooperative binding of Zn(II) ions with C-phycocyanin is observed. The binding constants diminished with increasing ionic strength, suggesting an adaptive protective response. "Nonelectrostatic" and polyelectrolyte components of binding free energy for Ag+, Cu2+, Cr3+, Pb2+, Ni2+, and Zn2+–C-phycocyanin (Spirulina platensis) complexes are determined. It is shown that "nonelectrostatic" component of binding free energy is dominating at the metal–C-PC interaction, while the polyelectrolyte contribution being less important, and the "nonelectrostatic" forces contribution for Ag+–C-phycocyanin (Spirulina platensis) complexes exceeds that for other metal ions.

Published in American Journal of Nano Research and Applications (Volume 5, Issue 3-1)

This article belongs to the Special Issue Nanotechnologies

DOI 10.11648/j.nano.s.2017050301.12
Page(s) 5-8
Creative Commons

This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited.

Copyright

Copyright © The Author(s), 2024. Published by Science Publishing Group

Keywords

C-phycocyanin, Zn Ions, Binding Constant

References
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[11] E. Gelagutashvili, “Ch. 9. Biosorption of heavy metals by Spirulina Platensis and their Components,” in Plants and Microbes, P. Goyal, A. Chauhan, and P. Kaushik, Eds., Mumbai, 2014, pp. 154–174.
[12] E. Gelagutashvili, “Binding of heavy metals with C-Phycocyanin: A Comparison between equilibrium dialysis, fluorescence and absorption titration”, Am. J. Biomed. Life Sci., vol.1, pp. 12–16, 2013.
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  • APA Style

    Eteri Gelagutashvili. (2016). Cyanobacteria Spirulina Platensis Basic Protein C-Phycocyanin and Zn(II) Ions. American Journal of Nano Research and Applications, 5(3-1), 5-8. https://doi.org/10.11648/j.nano.s.2017050301.12

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    ACS Style

    Eteri Gelagutashvili. Cyanobacteria Spirulina Platensis Basic Protein C-Phycocyanin and Zn(II) Ions. Am. J. Nano Res. Appl. 2016, 5(3-1), 5-8. doi: 10.11648/j.nano.s.2017050301.12

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    AMA Style

    Eteri Gelagutashvili. Cyanobacteria Spirulina Platensis Basic Protein C-Phycocyanin and Zn(II) Ions. Am J Nano Res Appl. 2016;5(3-1):5-8. doi: 10.11648/j.nano.s.2017050301.12

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  • @article{10.11648/j.nano.s.2017050301.12,
      author = {Eteri Gelagutashvili},
      title = {Cyanobacteria Spirulina Platensis Basic Protein C-Phycocyanin and Zn(II) Ions},
      journal = {American Journal of Nano Research and Applications},
      volume = {5},
      number = {3-1},
      pages = {5-8},
      doi = {10.11648/j.nano.s.2017050301.12},
      url = {https://doi.org/10.11648/j.nano.s.2017050301.12},
      eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.nano.s.2017050301.12},
      abstract = {The interaction of Zn(II) ions with cyanobacteria Spirulina platensis basic protein C-phycocyanin (C-PC) is studied by fluorescence spectroscopy.Stern–Volmer quenching constant value for Zn(II)–C-PC is determined. The binding energy of Zn(II) ions with C-phycocyanin is determined using equilibrium dialysis and atomic absorption spectroscopy. Cooperative binding of Zn(II) ions with C-phycocyanin is observed. The binding constants diminished with increasing ionic strength, suggesting an adaptive protective response. "Nonelectrostatic" and polyelectrolyte components of binding free energy for Ag+, Cu2+, Cr3+, Pb2+, Ni2+, and Zn2+–C-phycocyanin (Spirulina platensis) complexes are determined. It is shown that "nonelectrostatic" component of binding free energy is dominating at the metal–C-PC interaction, while the polyelectrolyte contribution being less important, and the "nonelectrostatic" forces contribution for Ag+–C-phycocyanin (Spirulina platensis) complexes exceeds that for other metal ions.},
     year = {2016}
    }
    

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  • TY  - JOUR
    T1  - Cyanobacteria Spirulina Platensis Basic Protein C-Phycocyanin and Zn(II) Ions
    AU  - Eteri Gelagutashvili
    Y1  - 2016/09/14
    PY  - 2016
    N1  - https://doi.org/10.11648/j.nano.s.2017050301.12
    DO  - 10.11648/j.nano.s.2017050301.12
    T2  - American Journal of Nano Research and Applications
    JF  - American Journal of Nano Research and Applications
    JO  - American Journal of Nano Research and Applications
    SP  - 5
    EP  - 8
    PB  - Science Publishing Group
    SN  - 2575-3738
    UR  - https://doi.org/10.11648/j.nano.s.2017050301.12
    AB  - The interaction of Zn(II) ions with cyanobacteria Spirulina platensis basic protein C-phycocyanin (C-PC) is studied by fluorescence spectroscopy.Stern–Volmer quenching constant value for Zn(II)–C-PC is determined. The binding energy of Zn(II) ions with C-phycocyanin is determined using equilibrium dialysis and atomic absorption spectroscopy. Cooperative binding of Zn(II) ions with C-phycocyanin is observed. The binding constants diminished with increasing ionic strength, suggesting an adaptive protective response. "Nonelectrostatic" and polyelectrolyte components of binding free energy for Ag+, Cu2+, Cr3+, Pb2+, Ni2+, and Zn2+–C-phycocyanin (Spirulina platensis) complexes are determined. It is shown that "nonelectrostatic" component of binding free energy is dominating at the metal–C-PC interaction, while the polyelectrolyte contribution being less important, and the "nonelectrostatic" forces contribution for Ag+–C-phycocyanin (Spirulina platensis) complexes exceeds that for other metal ions.
    VL  - 5
    IS  - 3-1
    ER  - 

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Author Information
  • E. Andronikashvili Institute of Physics, I. Javakhishvili Tbilisi State University, Tbilisi, Georgia

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