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https://doi.org/10.5562/cca1955

An Effector of Hemoglobin Structure: The Guanosine 3', 5'-Triphosphate

Saeed Rezaei-Zarchi ; Department of Biology, Payame Noor University, Yazd, Iran
Saber Imani ; Chemical Injuries Research Center, Baqiyatallah University of Medical Sciences, Tehran, Iran
Safieh Soufian ; Department of Biology, Payame Noor University, Arak, Iran
Yunes Panahi ; Chemical Injuries Research Center, Baqiyatallah University of Medical Sciences, Tehran, Iran
Ali Akbar Saboury ; Institutes of Biochemistry and Biophysics, University of Tehran, Tehran, Iran
Mohammad Reza Arefi ; Department of Civil Engineering and Nano Research Center, Taft branch, Islamic Azad University,Taft, Iran


Puni tekst: engleski pdf 1.272 Kb

str. 59-62

preuzimanja: 1.097

citiraj


Sažetak

The effect of guanosine 3', 5'-triphosphate (GTP) on the hemoglobin structure was studied by UV-visible, fluorescence and circular dichroism (CD) spectroscopies, and cyclic voltammetry. UV-visible absorption spectra showed an increase in absorbance in the regions of 420 nm and 280 nm. Fluorescence spectra showed that the Trp fluorescence intensity increased upon excitation at 280 nm, when guanosine 3', 5'-triphosphate concentration was increased in hemoglobin solution. Along with the increased fluorescence intensity, a slightly shift of λmax was also observed toward the higher wavelengths. CD spectral analysis demonstrated a significant decrease in negative ellipsity in the region of 205–235 nm. After adding guanosine 3', 5'-triphosphate to the hemoglobin solution α-helix structure decreases by 20 % while β-sheet conformation increases by 9 %. The effects of GTP on hemoglobin resulted in a 61 mV shift in the cathodic and 40 mV for anodic peak of hemoglobin in the CD. Our data showed the change of secondary and tertiary structure of hemoglobin in the presence of guanosine 3', 5'-triphosphate. (doi: 10.5562/cca1955)

Ključne riječi

hemoglobin structure, guanosine 3', 5'-triphosphate

Hrčak ID:

80413

URI

https://hrcak.srce.hr/80413

Posjeta: 1.618 *