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111.
Katalin Tenger Petro Khoroshyy Gábor Rákhely László Zimányi 《Journal of bioenergetics and biomembranes》2010,42(2):125-133
Maturation of c-type cytochromes involves the covalent and stereospecific enzymatic attachment of a heme b via thioether linkages to two conserved cysteines within apocytochromes. Horse cytochrome c is readily matured into its native holoform in the cytoplasm of E. coli when co-expressed with yeast cytochrome c heme lyase. Here we report the low yield formation of holocytochrome with covalently attached heme also in the absence of
heme lyase. This is the first demonstration of in vivo maturation of a eukaryotic cytochrome c in a prokaryotic cytoplasm without the assistance by a dedicated enzymatic maturation system. The assembled cytochrome c can be oxidized by cytochrome c oxidase, indicating the formation of a functional protein. The absorption spectrum is typical of a low spin, six coordinated
c-type heme. Nevertheless, minor spectral differences relative to the native cytochrome c, deviation of the midpoint reduction potential and slightly altered kinetic parameters of the interaction with cytochrome
c oxidase emphasize the importance of cytochrome c heme lyase in folding cytochrome c into its native conformation. 相似文献
112.
The potential of reverse-phase high-performance liquid chromatography for the separation of closely related proteins has been investigated. Using an octadecasilyl silica stationary phase and a propanol/pyridine formate solvent system normal α- and β-chains of human hemoglobin have been separated from several of their respective mutant chains which differ by single amino acid residues only. The results suggest that reverse-phase high-performance liquid chromatography is a powerful tool for the separation of medium-sized proteins with minimal structural difference. 相似文献