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• W2012117249 endingPage "5459" @default.
• W2012117249 startingPage "5450" @default.
• W2012117249 abstract "The folding of reduced cytochrome c (redcyt c) is increasingly being recognized as undergoing a mechanism that deviates from a two-state process. In previous far-UV TRORD studies of redcyt c folding, a rapidly forming intermediate was attributed to the appearance of a molten-globule-like (MG) state [Chen, E., Goldbeck, R. A., and Kliger, D. S. (2003) J. Phys. Chem. A 107, 8149–8155]. A slow folding phase (>1 ms) was identified with the formation of native (N) secondary structure from that MG form. Here, using 0.65 mM SDS to induce the MG state in oxidized cytochrome c, folding of redcyt c was triggered with fast photoreduction and probed from early microseconds to milliseconds using far-UV TRORD spectroscopy. The kinetics of the reaction are described with a time constant of 50 ± 16 ms, which corresponds to 1 ± 0.6 ms upon extrapolation of the data to zero SDS concentration. The latter folding time is about 5 times faster than the calculated GuHCl-free time constant of 5.5 ± 1.4 ms for slow-phase folding obtained in our previous study. This ratio of rates would be consistent with a scenario in which 20–30% MG that is suggested to form in the fast phase of redcyt c folding in GuHCl is an obligatory intermediate. The native state forms from this obligatory intermediate with an observed rate, kf = fkMG→N, where f is the fractional population of MG and kMG→N is the microscopic rate for MG → N. Calculation and comparison of the m⧧/m values show agreement within the uncertainties between the SDS (∼0.5) and GuHCl (∼0.3) based redcyt c folding experiments, suggesting that the two experiments report on comparable intermediates. The m values were obtained from far-UV CD SDS titration experiments, from which calculated thermodynamic parameters allowed estimation of the reduction potential for the MG state to be ∼155 mV (−15 kJ/mol) vs NHE which, like the reduction potential for the native state, is more favorable than that for the unfolded protein." @default.
• W2012117249 created "2016-06-24" @default.
• W2012117249 creator A5045222853 @default.
• W2012117249 creator A5051920458 @default.
• W2012117249 creator A5067894240 @default.
• W2012117249 date "2008-04-17" @default.
• W2012117249 modified "2023-09-26" @default.
• W2012117249 title "The Folding Kinetics of the SDS-Induced Molten Globule Form of Reduced Cytochrome <i>c</i>" @default.
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• W2012117249 doi "https://doi.org/10.1021/bi702452u" @default.
• W2012117249 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/18416561" @default.

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