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 journalArticle

209 Citations (Scopus)

Abstract

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
Volume4
Issue number1
DOIs
StatePublished - Jan 1997

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Cytochromes c
Histidine
Raman Spectrum Analysis
Protein Folding
Flow measurement
Heme
Methionine
Raman scattering
Proteins
Ligands
Kinetics

ASJC Scopus subject areas

  • Biochemistry
  • Structural Biology
  • Genetics

Cite this

Folding of cytochrome c initiated by submillisecond mixing. / Takahashi, Satoshi; Yeh, Syun-Ru; Das, Tapan K.; Chan, Chi Kin; Gottfried, David S.; Rousseau, Denis L.

In: Nature Structural Biology, Vol. 4, No. 1, 01.1997, p. 44-50.

Research output: Contribution to journalArticle

Takahashi, Satoshi ; Yeh, Syun-Ru ; Das, Tapan K. ; Chan, Chi Kin ; Gottfried, David S. ; Rousseau, Denis L. / Folding of cytochrome c initiated by submillisecond mixing. In: Nature Structural Biology. 1997 ; Vol. 4, No. 1. pp. 44-50.
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