Influence of NaCl and sorbitol on the stability of conformations of cytochrome c

Influence of ionic (NaCl) and non-ionic (sorbitol) additives on structural transitions of cytochrome c was investigated by circular dichroism, optical and EPR spectroscopy. Transformations of cytochrome c, induced by the acidification of solution and temperature perturbation, were monitored in the h...

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Bibliographic Details
Published in:Biophysical chemistry 2008-06, Vol.135 (1), p.110-115
Main Authors: Bágeľová, J., Fedunová, D., Gažová, Z., Fabian, M., Antalík, M.
Format: Article
Language:English
Subjects:
Animals
Circular Dichroism
Cytochrome c
Cytochromes c - chemistry
Electron Spin Resonance Spectroscopy
Enzyme Stability
Heme ligands
Horses
Humans
Hydrogen-Ion Concentration
Molten globule
Protein Conformation
Protein stability
Sodium Chloride - chemistry
Sorbitol - chemistry
Spectrophotometry
Temperature
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Summary:Influence of ionic (NaCl) and non-ionic (sorbitol) additives on structural transitions of cytochrome c was investigated by circular dichroism, optical and EPR spectroscopy. Transformations of cytochrome c, induced by the acidification of solution and temperature perturbation, were monitored in the heme pocket together with changes in the secondary structure. NaCl and sorbitol exhibited antagonistic effect on the acid-induced transition of the protein. Sorbitol enhanced the stability of native conformation while NaCl destabilized this state. The midpoints of acid-induced transitions in the axial coordination of heme as well as in the secondary structure occurred nearly at the same pH values. However, temperature-induced transitions in the unfolding of the secondary structure were almost coincidental with the cleavage of Met80–Fe bond only in the sorbitol solutions. In the salt solution the Met80–Fe bond was markedly more labile than the secondary structure.
ISSN:0301-4622
1873-4200
DOI:10.1016/j.bpc.2008.03.010