Article
Stabilization of Pseudomonas aeruginosa cytochrome c(551) by systematic amino acid substitutions based on the structure of thermophilic Hydrogenobacter thermophilus cytochrome c(552).
The Journal of biological chemistry - 31 Dec 1999
Hasegawa J, Shimahara H, Mizutani M, Uchiyama S, Arai H, Ishii M, Kobayashi Y, Ferguson S J, Sambongi Y, Igarashi Y
Abstract excerpt
A heterologous overexpression system for mesophilic Pseudomonas aeruginosa holocytochrome c(551) (PA c(551)) was established using Escherichia coli as a host organism. Amino acid residues were systematically substituted in three regions of PA c(551) with the corresponding residues from thermophilic Hydrogenobacter thermophilus cytochrome c(552) (HT c(552)), which has similar main chain folding to PA c(551), but...
Topics
- Amino Acid Substitution
- Bacteria
- Bacterial Proteins
- Cytochrome c Group
- Enzyme Stability
- Guanidine
- Magnetic Resonance Spectroscopy
- Mutation
- Protein Conformation
- Protein Denaturation
- Pseudomonas aeruginosa