Folding intermediates in cytochrome C

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94 Citations (Scopus)

Abstract

Folding of cytochrome c from its low pH guanidine hydrochloride (Gdn- HCI) denatured state revealed a new intermediate, a five-coordinate high spin species with a water molecule coordinated to the heme. Incorporation of this five-coordinated intermediate into the previously reported ligand exchange model can quantitatively account for the observed folding kinetics. In this new model, unfolded cytochrome c is converted to its native structure through an obligatory folding intermediate, the histidine-water coordination state, whereas the five-coordinate state and a bis-histidine state are off-pathway intermediates. When the concentration of Gdn-HCI in the refolding solution was increased, an acceleration of the conversion from the bis-histidine coordinated state to the histidine-water coordinated state was observed, demonstrating that the reaction requires unfolding of the mis-organized polypeptide structure associated with the bis-histidine state.

Original languageEnglish (US)
Pages (from-to)222-228
Number of pages7
JournalNature Structural Biology
Volume5
Issue number3
DOIs
StatePublished - 1998

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Cytochromes
Histidine
Cytochromes c
Water
Guanidine
Human computer interaction
Heme
Ligands
Peptides
Molecules
Kinetics

ASJC Scopus subject areas

  • Biochemistry
  • Structural Biology
  • Genetics

Cite this

Folding intermediates in cytochrome C. / Yeh, Syun-Ru; Rousseau, Denis L.

In: Nature Structural Biology, Vol. 5, No. 3, 1998, p. 222-228.

Research output: Contribution to journalArticle

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