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

Biophysical Chemistry
J Bágel'ováMarián Antalík

Abstract

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.

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Citations

Nov 21, 2013·Chemistry and Physics of Lipids·Julia Muenzner, Ekaterina V Pletneva
Jan 24, 2013·Proceedings of the National Academy of Sciences of the United States of America·Liam M LongoMichael Blaber
Jul 25, 2017·Journal of Molecular Graphics & Modelling·Gurusamy MuneeswaranChandran Karunakaran

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