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Folding intermediates in cytochrome c

Nature Structural Biology volume 5, pages 222–228 (1998)Cite this article

Abstract

Folding of cytochrome c from its low pH guanidine hydrochloride (Gdn-HCl) 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-HCl 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.

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  1. Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, New York, 10461, USA

    Syun-Ru Yeh & Denis L. Rousseau

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  2. Denis L. Rousseau
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Correspondence to Syun-Ru Yeh.

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Yeh, SR., Rousseau, D. Folding intermediates in cytochrome c. Nat Struct Mol Biol 5, 222–228 (1998). https://doi.org/10.1038/nsb0398-222

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