Volume 5, Issue 3-1, May 2017, Page: 5-8
Cyanobacteria Spirulina Platensis Basic Protein C-Phycocyanin and Zn(II) Ions
Eteri Gelagutashvili, E. Andronikashvili Institute of Physics, I. Javakhishvili Tbilisi State University, Tbilisi, Georgia
Received: Jul. 21, 2016;       Accepted: Jul. 25, 2016;       Published: Sep. 14, 2016
DOI: 10.11648/j.nano.s.2017050301.12      View  3353      Downloads  127
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.
C-phycocyanin, Zn Ions, Binding Constant
To cite this article
Eteri Gelagutashvili, Cyanobacteria Spirulina Platensis Basic Protein C-Phycocyanin and Zn(II) Ions, American Journal of Nano Research and Applications. Special Issue: Nanotechnologies. Vol. 5, No. 3-1, 2017, pp. 5-8. doi: 10.11648/j.nano.s.2017050301.12
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D. Bhattacharya and G. Rajinder, “Nanotechnology and potential of microorganisms”, Crit. Rev. Biotechnol., vol. 25, pp. 199–204, 2005.
K. Vijayaraghavan and S. P. Kamala Nalini, “Biotemplates in the green synthesis of silver nanoparticles”, Biotechnol. J., vol. 5, pp. 1098–1110, 2010.
M. Labrenz, G.K. Druschel, E.T. Thomsen, B. Gilbert, S.A. Welch, K.M. Kemner, G.A. Logan, R.E. Summons, G.D. Stasio, P.L. Bond, B. Lai, S.D. Kelly, and J.F. Banfield, “Formation of sphalerite (ZnS) deposits in natural biofilms of sulfate-reducing bacteria,” Science, vol. 290, pp. 1744–1747, 2000.
A.P. Philipse and D. Maas, “Magnetic colloids from magnetotactic bacteria: Chain formation and colloidal stability,” Langmuir, vol. 18, pp. 9977–9984, 2002.
M. Kowshik, W. Vogel, J. Urban, S.K. Kulkarni, and K.M. Paknikar, “Microbial synthesisof semiconductorPbS nanocrystallites,” Adv. Mater., vol. 14, pp. 815–818, 2002.
M. Kowshik, N. Deshmukh, S.K. Kulkarni, K.M. Paknikar, W. Vogel, and J. Urban, “Microbial synthesis of semiconductor CdS nanoparticles, their characterization, and their usein fabrication of an ideal diode,” Biotechnol. Bioeng., vol. 78, pp. 583–588, 2002.
O. Hayashi, S. Ono, K. Ishii, Y. Shi, T. Hirahashi, and T. Katoh, “Enhancement of proliferation and differentiation in bone marrow hematopoietic cells by Spirulina (Arthrospira) platensisin mice”, J. Appl. Phycology, vol. 18, pp. 47–56, 2006.
S.A. Kedik, E.I. Yartsev, I.V. Sakaeva, A.V. Panov, and E.S. Zhavoronok, “Influence of Spirulina andits component on the immune system”, Rus. J. Biopharmaceut., vol. 3, pp.3–10, 2011.
K.K.I.U. Arunakumara and Z. Xuecheng, “Effects of heavy metals (Pb2+ and Cd2+) on the ultra-structure, growth and pigment contents of the unicellular cyanobacterium Synechocystissp. PCC 6803”, Chin. J. Oceanol. Limnol.,vol. 27, pp. 383–388, 2009.
K.K.I.U. Arunakumara, Z. Xuecheng, and S. Xiaojin, “Bioaccumulation of Pb2+ and its effects on growth, morphology and pigment contents of Spirulina (Arthrospira) platensis,” J. Ocean Univ. Chin., vol. 7, pp. 397–403, 2008.
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.
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.
M.R. Eftinkand C.A. Ghiron, “Fluorescence quenching studies with proteins,” Anal. Biochem., vol. 114, pp. 199–227, 1981.
G. Scatchard, “The attraction of proteins for small molecules and ions,” Ann.N.Y.Acad. Sci., vol. 51, pp. 660–672, 1949.
A.V. Hill, “The possible effects of the aggregation of the molecules of hemoglobin on its dissociation curves”, J. Physiol., vol. 40, pp. 463–505, 1910.
Ch.R. Cantor, P.R. Shimmel, Biophysical Chemistry, Part III, Moscow: Mir, 1985.
N.T. Eriksen, “Production of phycocyanin – a pigment with applications in biology, biotechnology, foods and medicine,” Appl. Microbiol. Biotechnol., vol. 80, pp. 1–14, 2008.
A.M. Karshikov, M. Duerring, and R. Huber, “Role of electrostatic interaction in the stability of the hexamer of constitution phycocyanin from Fremyella dislosiphon,” Protein Eng., vol. 4, pp. 681–690, 1991.
M.T. Record and R.S. Spolar, “Some thermodynamic principles of nonspecific and site-specific protein-DNA interactions,” in The Biology of Nonspecific DNA-Protein Interactions, A. Revzin, Ed., Boca Raton: CRC Press, 1990, pp. 33–69.
M.T. Record, J.H. Ha, and M.A. Fisher, “Analysis of equilibrium and kinetic measurements to determine thermodynamic origins of stability and specificity and mechanism of formation of site-specific complexes between proteins and helical DNA,” Methods Enzymol., vol. 208, pp. 291–343, 1991.
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