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Influence of glycerol on the structure and redox properties of horse heart cytochrome c. A circular dichroism and electrochemical study.

Authors
  • De Sanctis, G
  • Maranesi, A
  • Ferri, T
  • Poscia, A
  • Ascoli, F
  • Santucci, R
Type
Published Article
Journal
Journal of Protein Chemistry
Publisher
Springer-Verlag
Publication Date
Oct 01, 1996
Volume
15
Issue
7
Pages
599–606
Identifiers
PMID: 8968951
Source
Medline
License
Unknown

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 alpha-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 (delta G0) 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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