Folding intermediates in cytochrome C

Research output: Contribution to journalArticle

94 Scopus citations

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 - Mar 25 1998

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Genetics

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