Folding of cytochrome c initiated by submillisecond mixing

Satoshi Takahashi, Syun Ru Yeh, Tapan K. Das, Chi Kin Chan, David S. Gottfried, Denis L. Rousseau

Research output: Contribution to journalArticlepeer-review

216 Scopus citations


Cytochrome c folding was initiated using a new solution mixer that provides a time window which covers over 90% of the burst phase unresolved by conventional stop-flow measurements. Folding was followed by resonance Raman scattering. Kinetic analysis of the high frequency Raman data indicates that a nascent phase occurs within the mixing dead time of 100 μs. A significant fraction of the protein was found to be trapped in a misfolded bis-histidine form during the nascent phase at pH 4.5, thereby preventing the protein from folding rapidly and homogeneously. The nascent phase was followed by a haem- ligand exchange phase that populates the native histidine-methionine coordinated form through a thermodynamically controlled equilibrium.

Original languageEnglish (US)
Pages (from-to)44-50
Number of pages7
JournalNature Structural Biology
Issue number1
StatePublished - Jan 1997

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Genetics


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