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Parallel pathways in cytochrome c(551) folding.

Stefano Gianni1, Carlo Travaglini-Allocatelli, Francesca Cutruzzolà

  • 1Istituto Pasteur-Fondazione Cenci Bolognetti, Dipartimento di Scienze Biochimiche e Istituto di Biologia e Patologia Molecolari del CNR, Università di Roma La Sapienza, Piazzale A. Moro 5, 00185 Rome, Italy.

Journal of Molecular Biology
|July 16, 2003
PubMed
Summary
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Cytochrome c(551) folding in Pseudomonas aeruginosa is complex, involving parallel pathways, not a simple sequential mechanism. Kinetic analysis reveals fast and slow folding routes, with methionine ligation occurring late in the dominant fast pathway.

Area of Science:

  • Biochemistry
  • Protein Folding Dynamics

Background:

  • Cytochrome c(551) from Pseudomonas aeruginosa was traditionally believed to fold via a simple sequential mechanism.
  • The absence of histidine residues, except for the native His16 heme ligand, supported the idea of no mis-coordinated species.

Purpose of the Study:

  • To investigate the folding mechanism of cytochrome c(551) beyond the previously assumed sequential model.
  • To identify complexities and alternative pathways in cytochrome c(551) folding.

Main Methods:

  • Double-jump interrupted refolding experiments at low pH.
  • Stopped-flow experiments monitoring absorbance at 695 nm.
  • Measurements on carboxymethylated cytochrome c(551).
  • Continuous-flow measurements of tryptophan-heme energy transfer.

Related Experiment Videos

  • Quantitative kinetic modeling.

    • Main Results:

    • Kinetic analysis revealed parallel folding pathways, contradicting the simple sequential model.
    • Approximately 50% of unfolded cytochrome c(551) uses a fast folding track (10 ms), while the remainder follows a slower path.
    • Methionine ligation occurs late in the fast folding track, dominant at physiological pH.
    • Rapid chain collapse (<100 μs) precedes the millisecond-timescale folding.
    • Evidence for a minor population folding via a parallel channel (10-50 ms).

    Conclusions:

    • Cytochrome c(551) folding involves at least two parallel pathways.
    • Denatured states exist as slowly inter-converting ensembles, influencing pH-dependent pathway selection.
    • The folding mechanism is more complex than previously understood, with distinct fast and slow routes.