Affiliation:
1. Department of Chemistry Faculty of Nano and Bio Science and Technology Persian Gulf University Bushehr 75169 Iran
2. Department of Chemical Industry Technical and Vocational University (TVU) Bushehr Iran
Abstract
AbstractUtilizing cytochrome c (Cyt c), we studied the covalent attachment of safranin O to a protein could affect the protein properties. The effect of covalent attachment of safranin to Cyt c was explored using spectroscopic techniques, which revealed changes in the secondary and tertiary structure of the protein. Using Trp 59 fluorescence emission (λem=355 nm) and safranin fluorescence profile (λem=587 nm), we investigated the changes in the structure of the heme moiety and the binding of safranin molecules to the Cyt c protein. Far‐UV CD spectroscopy results showed that modification significantly reduced the α‐helix content. Studies showed that the modification causes the prevention of thermal aggregation of the protein at 65 °C and decreases in the peroxidase activity of the protein. Investigating of the pH effect revealed that although the Cyt c modification reduced peroxidase activity, the pH shift to pH 6.0 could increase the peroxidase activity.