Comparative Analysis of Highly Homologous<i>Shewanella</i>Cytochromes<i>c</i><sub>5</sub>for Stability and Function

DOI Web Site Web Site 被引用文献9件 参考文献18件
  • TAKENAKA Satoshi
    Graduate School of Biosphere Science, Hiroshima University, CREST of Japan Science and Technology Corporation
  • WAKAI Satoshi
    Graduate School of Biosphere Science, Hiroshima University, CREST of Japan Science and Technology Corporation
  • TAMEGAI Hideyuki
    Department of Chemistry, College of Humanities and Sciences, Nihon University
  • UCHIYAMA Susumu
    Graduate School of Engineering, Osaka University
  • SAMBONGI Yoshihiro
    Graduate School of Biosphere Science, Hiroshima University, CREST of Japan Science and Technology Corporation

書誌事項

タイトル別名
  • Comparative Analysis of Highly Homologous Shewanella Cytochromes c5 for Stability and Function

この論文をさがす

抄録

Homologous cytochromes c5 from a mesophile, Shewanella amazonensis (SA cytc5), and a psychrophile, Shewanella violacea (SV cytc5), were compared to elucidate the molecular mechanisms underlying protein stability and function. Cyclic voltammetry revealed that the two proteins had the same redox potential value. Differential scanning calorimetry showed that SV cytc5 was more stable than SA cytc5 in an enthalpic manner. These results and the structure model of Shewanella oneidensis cytochrome c5 indicated that hydrophobic heme environments in the two proteins are the same to maintain the same redox potential value, and that the intra-molecular interactions in SV cytc5, perhaps involved in Lys-50 and Tyr-73, account for its higher stability. Electron transfer from SV cytc5 to membrane proteins of S. violacea and S. amazonensis was faster than that from SA cytc5, suggesting that solvent-exposed Lys-4 in SV cytc5 is responsible for the faster association and dissociation between SV cytc5 and its redox partner.

収録刊行物

被引用文献 (9)*注記

もっと見る

参考文献 (18)*注記

もっと見る

キーワード

詳細情報 詳細情報について

問題の指摘

ページトップへ