PMID: 9540804Apr 16, 1998Paper

A stable, molten-globule-like cytochrome c

Biochimica Et Biophysica Acta
P Wittung-Stafshede

Abstract

Expression of cytochrome c from Thermus thermophilus in Escherichia coli (E. coli) leads to a protein with characteristics of a molten globule. Unfolding induced by guanidine hydrochloride (GdHCl) shows that E. coli-expressed cytochrome c has lower stability (and less cooperativity of unfolding) compared to the protein extracted from Thermus thermophilus, even though the two proteins have identical amino-acid sequences. Moreover, Soret and far-UV circular dichroism signals differ for the two proteins, suggesting a distorted heme environment and more side-chain dynamics of E. coli-expressed cytochrome c. Still, tryptophan fluorescence in E. coli-expressed cytochrome c is quenched as in native protein, and the iron coordinates in a low-spin form. Amino-acid sequencing indicates the presence of only one covalent cysteine-linkage to the heme in E. coli-expressed cytochrome c (normally, there are two linkages), a possible explanation for the trapped, molten-globule-like structure. The features of this non-native protein may be of interest for interpretation of cytochrome c folding kinetics in vitro, since a molten globule may be an intermediate on the folding pathway.

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Citations

Apr 26, 2013·Cellular and Molecular Life Sciences : CMLS·Sobia ZaidiFaizan Ahmad
May 3, 2000·Proceedings of the National Academy of Sciences of the United States of America·E J Tomlinson, S J Ferguson
May 2, 2002·Biochimica Et Biophysica Acta·Ali Sabahi, Pernilla Wittung-Stafshede
May 15, 2015·Protein Science : a Publication of the Protein Society·Teresa MilettiAnthony Mittermaier
Jan 27, 2000·Structure·P D Barker, S J Ferguson
Jul 21, 1999·Brazilian Journal of Medical and Biological Research = Revista Brasileira De Pesquisas Médicas E Biológicas·N F Martins, M M Santoro
Apr 17, 2002·Accounts of Chemical Research·Pernilla Wittung-Stafshede

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