Selected mutations in a mesophilic cytochrome c confer the stability of a thermophilic counterpart

Mesophilic cytochrome c(551) of Pseudomonas aeruginosa (PA c(551)) became as stable as its thermophilic counterpart, Hydrogenobacter thermophilus cytochrome c(552) (HT c(552)), through only five amino acid substitutions. The five residues, distributed in three spatially separated regions, were selec...

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Veröffentlicht in:	The Journal of biological chemistry 2000-12, Vol.275 (48), p.37824-37828
Hauptverfasser:	Hasegawa, J, Uchiyama, S, Tanimoto, Y, Mizutani, M, Kobayashi, Y, Sambongi, Y, Igarashi, Y
Format:	Artikel
Sprache:	eng
Schlagworte:	Bacteria - enzymology Bacterial Proteins Cytochrome c Group - chemistry Cytochrome c Group - genetics Cytochrome c Group - metabolism Enzyme Stability Hydrogenobacter thermophilus Mutation Nuclear Magnetic Resonance, Biomolecular Protein Conformation Protein Denaturation Pseudomonas aeruginosa Pseudomonas aeruginosa - enzymology Temperature
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