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.
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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 |
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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. |
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Copyright © The Author(s), 2016. Published by Science Publishing Group |
C-phycocyanin, Zn Ions, Binding Constant
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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
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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Download@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}
}
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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