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Abstract
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Utilizing 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.
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