The protein-folding speed limit: Intrachain diffusion times set by electron-transfer rates in denatured Ru(NH3)5(His-33)-Zn-cytochrome c
AUTOR(ES)
Chang, I-Jy
FONTE
The National Academy of Sciences
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=153008Documentos Relacionados
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