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Home / Equine Research Bank / Protein Sci / The redox couple of the cytochrome c cyanide complex: the co...
Protein science : a publication of the Protein Society2006; 15(2); 234-241; doi: 10.1110/ps.051825906

The redox couple of the cytochrome c cyanide complex: the contribution of heme iron ligation to the structural stability, chemical reactivity, and physiological behavior of horse cytochrome c.

Abstract: Contrary to most heme proteins, ferrous cytochrome c does not bind ligands such as cyanide and CO. In order to quantify this observation, the redox potential of the ferric/ferrous cytochrome c-cyanide redox couple was determined for the first time by cyclic voltammetry. Its E0' was -240 mV versus SHE, equivalent to -23.2 kJ/mol. The entropy of reaction for the reduction of the cyanide complex was also determined. From a thermodynamic cycle that included this new value for the cyt c cyanide complex E0', the binding constant of cyanide to the reduced protein was estimated to be 4.7 x 10(-3) L M(-1) or 13.4 kJ/mol (3.2 kcal/mol), which is 48.1 kJ/mol (11.5 kcal/mol) less favorable than the binding of cyanide to ferricytochrome c. For coordination of cyanide to ferrocytochrome c, the entropy change was earlier experimentally evaluated as 92.4 J mol(-1) K(-1) (22.1 e.u.) at 25 K, and the enthalpy change for the same net reaction was calculated to be 41.0 kJ/mol (9.8 kcal/mol). By taking these results into account, it was discovered that the major obstacle to cyanide coordination to ferrocytochrome c is enthalpic, due to the greater compactness of the reduced molecule or, alternatively, to a lower rate of conformational fluctuation caused by solvation, electrostatic, and structural factors. The biophysical consequences of the large difference in the stabilities of the closed crevice structures are discussed.
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Publication Date: 2006-01-26 PubMed ID: 16434742PubMed Central: PMC2242453DOI: 10.1110/ps.051825906Google Scholar: Lookup
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Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

This research study explores the chemical reactivity, structural stability, and physiological behavior of horse cytochrome c, focusing specifically on its interaction with cyanide. Unlike most heme proteins, which bind ligands such as cyanide and CO, ferrous cytochrome c does not. To explain and quantify this anomaly, the research outlines a thermodynamic cycle that includes the redox potential of the ferric/ferrous cytochrome c-cyanide redox couple.

Redox Potential Determination

  • The research started by determining the redox potential of the ferric/ferrous cytochrome c-cyanide redox couple. This involved applying cyclic voltammetry.
  • Eventually, it was found to be -240 mV versus SHE, the standard hydrogen electrode, equivalent to -23.2 kJ/mol.
  • This measurement made it possible to compare the redox potential of this specific redox couple to others.

Entropy of Reaction and Cyanide Binding Constant

  • The researchers also determined the entropy of reaction for the reduction of the cyanide complex.
  • Including this new value in a thermodynamic cycle, the cyanide binding constant to the reduced protein was estimated to be 4.7 x 10(-3) L M(-1) or 13.4 kJ/mol (3.2 kcal/mol).
  • Interestingly, this value is notably less favorable than the binding of cyanide to ferricytochrome c by 48.1 kJ/mol (11.5 kcal/mol).

Entropy Change and Enthalpy Change for Cyanide Coordination

  • For cyanide coordination to ferrocytochrome c, parameters such as the entropy change and enthalpy change were evaluated.
  • The entropy change was found to be 92.4 J mol(-1) K(-1) (22.1 e.u.) at 25 K, while the enthalpy change for the same net reaction was calculated to be 41.0 kJ/mol (9.8 kcal/mol).
  • These results revealed that the biggest barrier to cyanide coordination to ferrocytochrome c is enthalpic, resulting from the increased compactness of the reduced molecule or the reduced rate of conformational fluctuation caused by factors such as solvation, electrostatic, and structural elements.

Implications of Findings

  • The research also delved into the biophysical consequences of the significant difference in the stability of the closed crevice structures.
  • Understanding the behavior of cytochrome c can enhance our understanding of energy production in cells, and possibly find implication in the development of novel therapies for various diseases.

Cite This Article

APA
Schejter A, Ryan MD, Blizzard ER, Zhang C, Margoliash E, Feinberg BA. (2006). The redox couple of the cytochrome c cyanide complex: the contribution of heme iron ligation to the structural stability, chemical reactivity, and physiological behavior of horse cytochrome c. Protein Sci, 15(2), 234-241. https://doi.org/10.1110/ps.051825906

Publication

Protein science : a publication of the Protein Society
ISSN: 0961-8368
NlmUniqueID: 9211750
Country: United States
Language: English
Volume: 15
Issue: 2
Pages: 234-241

Researcher Affiliations

Schejter, Abel
  • Sackler Institute of Molecular Medicine, Sackler Medical School, Tel-Aviv University, Tel-Aviv 69978, Israel. molec03@post.tau.ac.il
Ryan, Michael D
    Blizzard, Erica R
      Zhang, Chongyao
        Margoliash, Emanuel
          Feinberg, Benjamin A

            MeSH Terms

            • Animals
            • Cyanides / metabolism
            • Cytochromes c / chemistry
            • Cytochromes c / metabolism
            • Entropy
            • Heme / metabolism
            • Horses
            • Iron / metabolism
            • Oxidation-Reduction
            • Protein Conformation
            • Static Electricity
            • Thermodynamics

            Grant Funding

            • GM 55892 / NIGMS NIH HHS

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