Masanari Misa, Wakai Satoshi, Tamegai Hideyuki, Kurihara Tatsuo, Kato Chiaki, Sambongi Yoshihiro
Graduate School of Biosphere Science, Hiroshima University.
Biosci Biotechnol Biochem. 2011;75(9):1859-61. doi: 10.1271/bbb.110370. Epub 2011 Sep 7.
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.
耐压的利文斯顿希瓦氏菌（SL cytc₅）的细胞色素c₅比耐高压的紫色希瓦氏菌的高度同源对应物表现出更低的热稳定性。这种稳定性差异归因于一种焓效应，该效应可归因于第50位的氨基酸残基（亮氨酸或赖氨酸）。这些细胞色素c₅蛋白是理解蛋白质稳定性机制的合适材料。
