Keywords

Hemoglobin Cytochrome C Protein Unfolding

Abstract

The unfolding behavior of two heme proteins, hemoglobin (Hb) and cytochrome c (Cyt c), was studied using UV-visible absorption and fluorescence spectroscopy. Chemical denaturants guanidine hydrochloride (GdHCl) and urea (Urea) were used to induce conformational unfolding of two proteins, and the unfolding mechanisms of the two proteins were elucidated. The heme (Heme) prosthetic group of Hb coordinates with the porphyrin iron atom and histidine, and the stability of the bond with the peptide chain is poor, and it dissociates under the action of 3.0 mol/L guanidine hydrochloride. The Heme prosthetic group of Cyt c exhibits strong stability through the disulfide bond formed by porphyrin and cysteine, and it is difficult to dissociate even if the concentration of guanidine hydrochloride reaches 6.0 mol/L. This study provides an important basis for elucidating the relationship between protein conformation and function.

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Original research done by Qiao Mengxia, Fan Suhua, Song Yanling, Zhang Hong, Wu Hai, Shen Fangming, Zheng Tiantian

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