The protein-folding speed limit: Intrachain diffusion times set by electron-transfer rates in denatured Ru(NH3)5(His-33)-Zn-cytochrome c

I. Jy Chang, Jennifer C. Lee, Jay R. Winkler, Harry B. Gray

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Abstract

The kinetics of electron transfer from the triplet-excited Zn-porphyrin to a Ru(NH3)5(His-33)3+ complex have been measured in Zn-substituted ruthenium-modified cytochrome c under denaturing conditions. In the folded protein, the electron-tunneling rate constant is 7.5 × 105 s-1. As the protein is denatured with guanidine hydrochloride, a faster adiabatic electron-transfer reaction appears (4.0 × 106 s-1, [guanidine hydrochloride] = 5.4 M) that is limited by the rate of intrachain diffusion to bring the Zn-porphyrin and Ru complex into contact. The 250-ns contact time for formation of a 15-residue loop in denatured cytochrome c is in accord with a statistical model developed by Camacho and Thirumalai [Camacho, C. J. & Thirumalai, D. (1995) Proc. Natl. Acad. Sci. USA 92, 1277-1281] that predicts that the most probable transient loops formed in denatured proteins are comprised of 10 amino acids. Extrapolation of the cytochrome c contact time to a 10-residue loop sets the folding speed limit at ≈107 s-1.

Original languageEnglish
Pages (from-to)3838-3840
Number of pages3
JournalProceedings of the National Academy of Sciences of the United States of America
Volume100
Issue number7
DOIs
Publication statusPublished - 2003 Apr 1

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Protein Folding
Cytochromes c
Guanidine
Porphyrins
Electrons
Proteins
Ruthenium
Statistical Models
Amino Acids
Ru(NH3)(5)His(33)-zn-cytochrome c

ASJC Scopus subject areas

  • General

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The protein-folding speed limit : Intrachain diffusion times set by electron-transfer rates in denatured Ru(NH3)5(His-33)-Zn-cytochrome c. / Chang, I. Jy; Lee, Jennifer C.; Winkler, Jay R.; Gray, Harry B.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 100, No. 7, 01.04.2003, p. 3838-3840.

Research output: Contribution to journalArticle

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