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Related Experiment Videos

Folding intermediates in cytochrome c

S R Yeh1, D L Rousseau

  • 1Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, New York 10461, USA. SYEH@AECOM.YU.EDU

Nature Structural Biology
|March 21, 1998
PubMed
Summary
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Researchers discovered a new intermediate in cytochrome c folding, a five-coordinate high spin species. This finding refines our understanding of protein folding kinetics and intermediate states.

Area of Science:

  • Biochemistry
  • Protein Folding Dynamics
  • Spectroscopy

Background:

  • Cytochrome c folding is a complex process involving multiple intermediate states.
  • Previous models did not fully account for all observed folding kinetics.

Purpose of the Study:

  • To identify and characterize novel intermediates in cytochrome c folding.
  • To refine existing models of protein folding kinetics.

Main Methods:

  • Low pH guanidine hydrochloride (Gdn-HCl) denaturation and refolding experiments.
  • Spectroscopic analysis to identify heme coordination states.

Main Results:

  • A new five-coordinate high spin intermediate with a water-coordinated heme was identified.

Related Experiment Videos

  • This intermediate, when incorporated into a ligand exchange model, quantitatively explains folding kinetics.
  • The histidine-water coordination state is an obligatory intermediate, while the five-coordinate and bis-histidine states are off-pathway.

    • Conclusions:

    • The newly identified five-coordinate intermediate is crucial for accurately modeling cytochrome c folding.
    • Increased Gdn-HCl concentration accelerates the conversion from the bis-histidine to the histidine-water state, indicating unfolding is required.
    • This study provides a more comprehensive understanding of cytochrome c folding pathways and intermediate roles.