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Ferro-chelatase enzyme activity of blue green algae from Yeşilırmak

Year 2020, , 72 - 78, 26.08.2020

Vahit Konar , Önder İdil , Emine Çelikoğlu , Umut Çelikoğlu

https://doi.org/10.38058/ijsl.768264

Abstract

Blue green algae are microscopic photosynthetic bacteria, naturally in ponds, rivers, lakes and streams. Tetra pyrroles can be classified based on the presence, position and substituents of a chelated metal in the pyrrole ring. Heme and chlorophyll, which are the most common tetra pyrolle in nature, are synthesized by blue green algae. Heme is an essential cofactor for virtually all forms of life and the last step of heme biosynthesis is catalyzed by ferrochelatase enzyme. In this study, blue green algae, photosynthetic bacteria, isolated from Yeşilırmak were used. Eight morphologically different isolates were obtained. The highest specific activity belongs to isolate 8 as 0.217 Umg-1.

Keywords

Blue green algae Ferro-chelatase Tetra pyrrole Yeşilırmak

Supporting Institution

Amasya University

Project Number

FMB-BAP 18-0348

References

  • Al-Karadaghi, S., Hansson, M., Nikonov, S., Jönsson, B., & Hederstedt, L. 1997. Crystal structure of ferrochelatase: the terminal enzyme in heme biosynthesis. Structure, 5(11), 1501-1510.
  • Beale, S. I. 1994. Biosynthesis of cyanobacterial tetrapyrrole pigments: hemes, chlorophylls, and phycobilins. In the molecular biology of cyanobacteria (pp. 519-558). Springer, Dordrecht.
  • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical biochemistry, 72(1-2), 248-254.
  • Camadro, J. M., & Labbe, P. 1988. Purification and properties of ferrochelatase from the yeast Saccharomyces cerevisiae. Evidence for a precursor form of the protein. Journal of Biological Chemistry, 263(24), 11675-11682.
  • Cánepa, E. T., & Llambías, E. B. 1988. Purification and characterization of ferro-and cobalto-chelatases. Biochemistry and Cell Biology, 66(1), 32-39.
  • Dailey Jr, H. A., & Lascelles, J. 1974. Ferrochelatase activity in wild-type and mutant strains of Spirillum itersonii: Solubilization with chaotropic reagents. Archives of biochemistry and biophysics, 160(2), 523-529.
  • Dailey, H. A. 1982. Purification and characterization of membrane-bound ferrochelatase from Rhodopseudomonas sphaeroides. Journal of Biological Chemistry, 257(24), 14714-14718.
  • Dailey, H. A. (Ed.). 1990. Biosynthesis of heme and chlorophylls. McGraw-Hill Companies.
  • Franco, R., Moura, J. J., Moura, I., Lloyd, S. G., Huynh, B. H., Forbes, W. S., & Ferreira, G. C. 1995. Characterization of the iron-binding site in mammalian ferrochelatase by kinetic and Mössbauer methods. Journal of Biological Chemistry, 270(44), 26352-26357.
  • Goldin, B. R., & Little, H. N. 1969. Metalloporphyrin chelatase from barley. Biochimica et Biophysica Acta (BBA)-Enzymology, 171(2), 321-332.
  • Hardison, R. 1999. The evolution of hemoglobin: studies of a very ancient protein suggest that changes in gene regulation are an important part of the evolutionary story. American Scientist, 87(2), 126-137.
  • Ivleva, N. B., & Golden, S. S. 2007. Protein extraction, fractionation, and purification from cyanobacteria. In Circadian rhythms (pp. 365-373). Humana Press.
  • Jones, O. T. G. 1968. Ferrochelatase of spinach chloroplasts. Biochemical Journal, 107(1), 113-119.
  • Kobayashi, K., Mochizuki, N., Yoshimura, N., Motohashi, K., Hisabori, T., & Masuda, T. 2008. Functional analysis of Arabidopsis thaliana isoforms of the Mg-chelatase CHLI subunit. Photochemical & Photobiological Sciences, 7(10), 1188-1195.
  • Matringe, M., Camadro, J. M., Joyard, J., & Douce, R. 1994. Localization of ferrochelatase activity within mature pea chloroplasts. Journal of Biological Chemistry, 269(21), 15010-15015.
  • Miyamoto, K., Kanaya, S., Morikawa, K., & Inokuchi, H. 1994. Overproduction, purification, and characterization of ferrochelatase from Escherichia coli. The Journal of Biochemistry, 115(3), 545-551.
  • Porra, R., & Jones, O. 1963. Studies on ferrochelatase. 1. Assay and properties of ferrochelatase from a pig-liver mitochondrial extract. Biochemical Journal, 87(1), 181.
  • Suzuki, T., Masuda, T., Singh, D. P., Tan, F. C., Tsuchiya, T., Shimada, H., ... & Takamiya, K. I. 2002. Two types of ferrochelatase in photosynthetic and nonphotosynthetic tissues of cucumber their difference in phylogeny, gene expression, and localization. Journal of Biological Chemistry, 277(7), 4731-4737.

Year 2020, , 72 - 78, 26.08.2020

Vahit Konar , Önder İdil , Emine Çelikoğlu , Umut Çelikoğlu

https://doi.org/10.38058/ijsl.768264

Abstract

Project Number

FMB-BAP 18-0348

References

  • Al-Karadaghi, S., Hansson, M., Nikonov, S., Jönsson, B., & Hederstedt, L. 1997. Crystal structure of ferrochelatase: the terminal enzyme in heme biosynthesis. Structure, 5(11), 1501-1510.
  • Beale, S. I. 1994. Biosynthesis of cyanobacterial tetrapyrrole pigments: hemes, chlorophylls, and phycobilins. In the molecular biology of cyanobacteria (pp. 519-558). Springer, Dordrecht.
  • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical biochemistry, 72(1-2), 248-254.
  • Camadro, J. M., & Labbe, P. 1988. Purification and properties of ferrochelatase from the yeast Saccharomyces cerevisiae. Evidence for a precursor form of the protein. Journal of Biological Chemistry, 263(24), 11675-11682.
  • Cánepa, E. T., & Llambías, E. B. 1988. Purification and characterization of ferro-and cobalto-chelatases. Biochemistry and Cell Biology, 66(1), 32-39.
  • Dailey Jr, H. A., & Lascelles, J. 1974. Ferrochelatase activity in wild-type and mutant strains of Spirillum itersonii: Solubilization with chaotropic reagents. Archives of biochemistry and biophysics, 160(2), 523-529.
  • Dailey, H. A. 1982. Purification and characterization of membrane-bound ferrochelatase from Rhodopseudomonas sphaeroides. Journal of Biological Chemistry, 257(24), 14714-14718.
  • Dailey, H. A. (Ed.). 1990. Biosynthesis of heme and chlorophylls. McGraw-Hill Companies.
  • Franco, R., Moura, J. J., Moura, I., Lloyd, S. G., Huynh, B. H., Forbes, W. S., & Ferreira, G. C. 1995. Characterization of the iron-binding site in mammalian ferrochelatase by kinetic and Mössbauer methods. Journal of Biological Chemistry, 270(44), 26352-26357.
  • Goldin, B. R., & Little, H. N. 1969. Metalloporphyrin chelatase from barley. Biochimica et Biophysica Acta (BBA)-Enzymology, 171(2), 321-332.
  • Hardison, R. 1999. The evolution of hemoglobin: studies of a very ancient protein suggest that changes in gene regulation are an important part of the evolutionary story. American Scientist, 87(2), 126-137.
  • Ivleva, N. B., & Golden, S. S. 2007. Protein extraction, fractionation, and purification from cyanobacteria. In Circadian rhythms (pp. 365-373). Humana Press.
  • Jones, O. T. G. 1968. Ferrochelatase of spinach chloroplasts. Biochemical Journal, 107(1), 113-119.
  • Kobayashi, K., Mochizuki, N., Yoshimura, N., Motohashi, K., Hisabori, T., & Masuda, T. 2008. Functional analysis of Arabidopsis thaliana isoforms of the Mg-chelatase CHLI subunit. Photochemical & Photobiological Sciences, 7(10), 1188-1195.
  • Matringe, M., Camadro, J. M., Joyard, J., & Douce, R. 1994. Localization of ferrochelatase activity within mature pea chloroplasts. Journal of Biological Chemistry, 269(21), 15010-15015.
  • Miyamoto, K., Kanaya, S., Morikawa, K., & Inokuchi, H. 1994. Overproduction, purification, and characterization of ferrochelatase from Escherichia coli. The Journal of Biochemistry, 115(3), 545-551.
  • Porra, R., & Jones, O. 1963. Studies on ferrochelatase. 1. Assay and properties of ferrochelatase from a pig-liver mitochondrial extract. Biochemical Journal, 87(1), 181.
  • Suzuki, T., Masuda, T., Singh, D. P., Tan, F. C., Tsuchiya, T., Shimada, H., ... & Takamiya, K. I. 2002. Two types of ferrochelatase in photosynthetic and nonphotosynthetic tissues of cucumber their difference in phylogeny, gene expression, and localization. Journal of Biological Chemistry, 277(7), 4731-4737.
There are 18 citations in total.

Details

Primary Language English
Journal Section Research Articles
Authors

Vahit Konar 0000-0002-5462-2505

Önder İdil 0000-0003-1744-4006

Emine Çelikoğlu 0000-0002-5956-0008

Umut Çelikoğlu 0000-0003-0995-8154

Project Number FMB-BAP 18-0348
Publication Date August 26, 2020
Published in Issue Year 2020

Cite

APA Konar, V., İdil, Ö., Çelikoğlu, E., Çelikoğlu, U. (2020). Ferro-chelatase enzyme activity of blue green algae from Yeşilırmak. International Journal of Science Letters, 2(2), 72-78. https://doi.org/10.38058/ijsl.768264
AMA Konar V, İdil Ö, Çelikoğlu E, Çelikoğlu U. Ferro-chelatase enzyme activity of blue green algae from Yeşilırmak. IJSL. August 2020;2(2):72-78. doi:10.38058/ijsl.768264
Chicago Konar, Vahit, Önder İdil, Emine Çelikoğlu, and Umut Çelikoğlu. “Ferro-Chelatase Enzyme Activity of Blue Green Algae from Yeşilırmak”. International Journal of Science Letters 2, no. 2 (August 2020): 72-78. https://doi.org/10.38058/ijsl.768264.
EndNote Konar V, İdil Ö, Çelikoğlu E, Çelikoğlu U (August 1, 2020) Ferro-chelatase enzyme activity of blue green algae from Yeşilırmak. International Journal of Science Letters 2 2 72–78.
IEEE V. Konar, Ö. İdil, E. Çelikoğlu, and U. Çelikoğlu, “Ferro-chelatase enzyme activity of blue green algae from Yeşilırmak”, IJSL, vol. 2, no. 2, pp. 72–78, 2020, doi: 10.38058/ijsl.768264.
ISNAD Konar, Vahit et al. “Ferro-Chelatase Enzyme Activity of Blue Green Algae from Yeşilırmak”. International Journal of Science Letters 2/2 (August 2020), 72-78. https://doi.org/10.38058/ijsl.768264.
JAMA Konar V, İdil Ö, Çelikoğlu E, Çelikoğlu U. Ferro-chelatase enzyme activity of blue green algae from Yeşilırmak. IJSL. 2020;2:72–78.
MLA Konar, Vahit et al. “Ferro-Chelatase Enzyme Activity of Blue Green Algae from Yeşilırmak”. International Journal of Science Letters, vol. 2, no. 2, 2020, pp. 72-78, doi:10.38058/ijsl.768264.
Vancouver Konar V, İdil Ö, Çelikoğlu E, Çelikoğlu U. Ferro-chelatase enzyme activity of blue green algae from Yeşilırmak. IJSL. 2020;2(2):72-8.