抄録
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.