Influence of glycerol on the structure and redox properties of horse heart cytochrome c. A circular dichroism and electrochemical study |
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Authors: | Giampiero De Sanctis Alessandra Maranesi Tommaso Ferri Alessandro Poscia Franca Ascoli and Roberto Santucci |
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Institution: | (1) Department of Biology M.C.A., University of Camerino, Camerino, Italy;(2) Department of Chemistry, University of Rome La Sapienza, Rome, Italy;(3) Department of Experimental Medicine and Biochemical Sciences, University of Rome Tor Vergata, Rome, Italy |
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Abstract: | The effect of glycerol on the structure and redox properties of horse heart cytochrome c was investigated by absorption spectroscopy, circular dichroism, and dc cyclic voltammetry techniques. The results show that the organic solvent increases the -helix structure of the protein and induces slight changes at the active-site environment; however, the overall tertiary structure does not appear to be significantly perturbed. Glycerol stabilizes cytochrome c, the free energy of denaturation (G
0) being approximately 0.7 kcal/mol larger than that determined in phosphate buffer under the same conditions, and influences the heterogeneous electron transfer kinetics at a chemically modified gold electrode; on the other hand, the redox potential of the protein is unaltered. On the whole, the results obtained indicate that glycerol acts as a suitable stabilizing agent of cytochrome c, which is of interest for application in biotechnology; the organic solvent does not alter the tertiary structure significantly or the redox properties of the protein. This has to be interpreted not only in terms of the glycerol-induced solvent ordering around the protein surface, but also as due to the specific features of the protein matrix. |
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Keywords: | Cytochrome c hemoprotein glycerol protein stabilization redox potential |
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