Effects of cysteine introduction into three homologous cytochromes C.
A cysteine residue was systematically introduced into three homologous cytochromes c from Hydrogenobacter thermophilus, Hydrogenophilus thermoluteolus, and Pseudomonas aeruginosa at a conserved position. The H. thermoluteolus variant showed the most decreased thermal stability as compared with the wild type, which might have been due in part to crosslinked polymer formation. The effects of cysteine introduction differed even at the conserved position in these homologous proteins.
Kobayashi
Yoshiko
Y
Graduate School of Biosphere Science, Hiroshima University, CREST of Japan Science and Technology Corporation, Hiroshima, Japan.
Sonoyama
Takafumi
T
Takeda
Taku
T
Sambongi
Yoshihiro
Y
D001419:Bacteria / Q000201:enzymology; D017124:Conserved Sequence; D003545:Cysteine; D045304:Cytochromes c / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D004795:Enzyme Stability; D008958:Models, Molecular; D009154:Mutation; D010084:Oxidation-Reduction; D011487:Protein Conformation; D011489:Protein Denaturation; D017386:Sequence Homology, Amino Acid; D013696:Temperature
D045304:Cytochromes c; D003545:Cysteine