title: Thermal stability of cytochrome c₅ of pressure-sensitive Shewanella livingstonensis.
abstract: Cytochrome c₅ of pressure-sensitive Shewanella livingstonensis (SL cytc₅) exhibits lower thermal stability than a highly homologous counterpart of pressure-tolerant Shewanella violacea. This stability difference is due to an enthalpic effect that can be attributed to the amino acid residue at position 50 (Leu or Lys). These cytc₅ proteins are appropriate materials for understanding the protein stability mechanism.
authors: Graduate School of Biosphere Science, Hiroshima University.
authors: Misa
authors: M
authors: Masanari
authors: Satoshi
authors: S
authors: Wakai
authors: Hideyuki
authors: H
authors: Tamegai
authors: Tatsuo
authors: T
authors: Kurihara
authors: Chiaki
authors: C
authors: Kato
authors: Yoshihiro
authors: Y
authors: Sambongi
mesh_terms: D000595:Amino Acid Sequence; D059001:Aquatic Organisms / Q000737:chemistry / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D003001:Cloning, Molecular; D003574:Cytochrome c Group / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D004795:Enzyme Stability; D004926:Escherichia coli; D008958:Models, Molecular; D008969:Molecular Sequence Data; D044367:Phase Transition; D010957:Plasmids; D011312:Pressure; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D020592:Shewanella / Q000737:chemistry / Q000201:enzymology*; D013696:Temperature; D013816:Thermodynamics; D014169:Transformation, Bacterial
chemical_list: D001426:Bacterial Proteins; D003574:Cytochrome c Group; D011994:Recombinant Proteins; C046450:cytochrome C5