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Home / Equine Research Bank / J Biol Inorg Chem / Correlation of acid-induced conformational transition of fer...
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2008; 13(5); 713-721; doi: 10.1007/s00775-008-0357-8

Correlation of acid-induced conformational transition of ferricytochrome c with cyanide binding kinetics.

Abstract: A relation between pH-induced conformational transitions of horse heart ferricytochrome c and the kinetics of external ligand coordination to heme iron was investigated by optical spectroscopy, circular dichroism and viscometry. The dependencies of both the association, k (a), and dissociation rate constants of cyanide binding on pH were determined from kinetic measurements. The association rate constant exhibits a bell-shaped form of dependence on pH in the region where this protein unfolds. The maximum of the dependence of k (a) on pH is found to be coincident with the pK values of conformational transitions of ferricytochrome c in solutions with both low and high ionic strengths. This observation is explained in terms of ferricytochrome c unfolding, which is characterized by two processes: the gradual opening of the heme crevice accompanied by the detachment of the axial Met80 and its replacement with a water molecule. The former process enhances the rate, whereas the latter results in the inhibition of the rate of cyanide binding.
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Publication Date: 2008-03-04 PubMed ID: 18317818DOI: 10.1007/s00775-008-0357-8Google Scholar: Lookup
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  • Journal Article
  • Research Support
  • Non-U.S. Gov't

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 study examined the connection between pH-triggered structural changes in the horse heart protein ferricytochrome c and how easily an external substance binds to its heme iron. The research found that the speed of cyanide binding depends on the solution’s pH, which also influences structural transitions in the protein.

Research Methodology

  • The researchers performed the study using optical spectroscopy, circular dichroism, and viscometry to observe how ferricytochrome c, a protein found in horse hearts, transforms under different pH conditions and how these transformations affect its ability to bind with cyanide molecules.
  • They estimated the association and disassociation rate constants of cyanide binding based on kinetic measurements, which showed how quickly the cyanide bound to or released from the protein.

Findings

  • The association rate constant displayed a bell-shaped dependence on pH, suggesting a peak rate of binding in the phase where the protein unfolds.
  • The maximum rate of binding correlated with the pK values (the logarithm of the dissociation constant) of structural changes in the ferricytochrome c, both in low- and high-saline solutions.

Interpretation of Results

  • The researchers hypothesized that these patterns occur due to the unfolding of ferricytochrome c, which consists of two parts: the gradual opening of the heme crevice and the displacement of the axial Met80 (a methionine amino acid molecule) with a water molecule.
  • The first part increases the rate of cyanide binding because the opening allows more accessible points for the cyanide molecule to attach. In contrast, the second part slows this binding process as the water molecule obstructs the cyanide’s access to the heme iron within the protein’s structure.

Cite This Article

APA
Varhac R, Antalík M. (2008). Correlation of acid-induced conformational transition of ferricytochrome c with cyanide binding kinetics. J Biol Inorg Chem, 13(5), 713-721. https://doi.org/10.1007/s00775-008-0357-8

Publication

Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry
ISSN: 0949-8257
NlmUniqueID: 9616326
Country: Germany
Language: English
Volume: 13
Issue: 5
Pages: 713-721

Researcher Affiliations

Varhac, Rastislav
  • Department of Biochemistry, Faculty of Science, P. J. Safárik University, Moyzesova 11, 04001, Kosice, Slovakia. rastislav.varhac@upjs.sk
Antalík, Marián

    MeSH Terms

    • Acids / chemistry
    • Animals
    • Circular Dichroism
    • Cyanides / metabolism
    • Cytochromes c / chemistry
    • Heme / chemistry
    • Horses
    • Hydrogen-Ion Concentration
    • Iron / chemistry
    • Kinetics
    • Myocardium / chemistry
    • Protein Binding
    • Protein Conformation
    • Spectrophotometry, Ultraviolet
    • Viscosity

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    Citations

    This article has been cited 2 times.
    1. Nugraheni AD, Nagao S, Yanagisawa S, Ogura T, Hirota S. Interaction of dimeric horse cytochrome c with cyanide ion.. J Biol Inorg Chem 2013 Mar;18(3):383-90.
      doi: 10.1007/s00775-013-0982-8pubmed: 23412550google scholar: lookup
    2. Sedlák E, Fabian M, Robinson NC, Musatov A. Ferricytochrome c protects mitochondrial cytochrome c oxidase against hydrogen peroxide-induced oxidative damage.. Free Radic Biol Med 2010 Nov 30;49(10):1574-81.
      doi: 10.1016/j.freeradbiomed.2010.08.019pubmed: 20801213google scholar: lookup
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