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Published November 9, 2005 | Supplemental Material
Journal Article Open

Nature of the Cytochrome c Molten Globule

Abstract

We have employed fluorescence energy transfer (FET) kinetics to probe unfolded and molten globule states of five dansyl (Dns) variants of Saccharomyces cerevisiae iso-1 cytochrome c. The covalently bound Fe(III) heme group quenches Dns fluorescence by energy transfer; measurements of FET kinetics yielded distributions of D−A distances (P(r)) for these states. The P(r) distributions and corresponding mean force potentials (U(r)) show that the cytochrome c molten globule is a highly structured state with a substantial number of native interactions. Wide P(r) distributions directly reflect the dynamic nature and conformational diversity of this molten globule. P(r) distributions for the "burst-phase" refolding intermediate suggest that the equilibrium cytochrome c molten globule is not a suitable model for early intermediates formed during protein refolding.

Additional Information

© 2005 American Chemical Society. Received 12 August 2005. Published online 13 October 2005. Published in print 1 November 2005. This work was supported by NIH GM068461 (J.R.W.) and the Ellison Medical Foundation (Senior Scholar Award in Aging to H.B.G.).

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