Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Dramatic stabilization of ferricytochrome c upon reduction

S Hilgen-Willis1, E F Bowden, G J Pielak

  • 1Department of Chemistry, University of North Carolina, Chapel Hill.

Journal of Inorganic Biochemistry
|August 15, 1993
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

X-ray structure of the metcyano form of dehaloperoxidase from Amphitrite ornata: evidence for photoreductive dissociation of the iron-cyanide bond.

Acta crystallographica. Section D, Biological crystallography·2010
Same author

Solvent-induced collapse of alpha-synuclein and acid-denatured cytochrome c.

Protein science : a publication of the Protein Society·2001
Same author

Characterization of horse cytochrome c expressed in Escherichia coli.

Protein expression and purification·2001
Same author

Interpreting the effects of small uncharged solutes on protein-folding equilibria.

Annual review of biophysics and biomolecular structure·2001
Same author

Second virial coefficients as a measure of protein--osmolyte interactions.

Protein science : a publication of the Protein Society·2001
Same author

Interactions between yeast iso-1-cytochrome c and its peroxidase.

Biochemistry·2001

Adding an electron significantly stabilizes ferricytochrome c (the oxidized form). This simple modification makes reduced cytochrome c one of the most stable proteins known.

Area of Science:

  • Biochemistry
  • Protein Stability
  • Biophysics

Background:

  • Cytochrome c is a crucial protein involved in electron transport.
  • Understanding protein stability is key to comprehending biological function.
  • The C102T variant of Saccharomyces cerevisiae iso-1-ferricytochrome c is a model system for studying protein behavior.

Purpose of the Study:

  • To determine the free energy of denaturation for the reduced (ferro) form of cytochrome c.
  • To investigate the impact of reduction (electron addition) on protein stability.
  • To compare the stability of oxidized and reduced cytochrome c.

Main Methods:

  • Combining measurements of free energy of denaturation for the oxidized (ferric) state.
  • Determining formal potentials for both native and chemically-denatured states.

Related Experiment Videos

  • Calculating the free energy of denaturation for the reduced (ferro) state.

    • Main Results:

    • Reduction of ferricytochrome c increases its stability by approximately 10 kcal mol-1 at 300 K and pH 4.6.
    • The ferro form of cytochrome c is exceptionally stable.
    • This stability enhancement is attributed to the addition of a single electron.

    Conclusions:

    • The reduction of cytochrome c confers significant thermodynamic stability.
    • Reduced cytochrome c represents one of the most stable proteins documented.
    • These findings provide insights into the intrinsic stability of proteins and the role of redox state.