Theoretical Study on Oligomerization of Cytochrome <i>c</i>

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  • MOTOKI Hideyoshi
    Department of Chemistry, Biology, and Marine Science, Graduate School of Engineering and Science,University of the Ryukyus, 1 Senbaru, Nishihara, Okinawa 903-0213, Japan
  • YOSHIDA Norio
    Department of Chemistry, Graduate School of Science, Kyushu University, 744 Motooka,Nishiku, Fukuoka 819-0395, Japan
  • HIROTA Shun
    Graduate School of Materials Science, Nara Institute of Science and Technology,8916-5 Takayama, Ikoma, Nara 630-0192, Japan
  • HIGASHI Masahiro
    Department of Chemistry, Biology, and Marine Science, Faculty of Science, University of the Ryukyus,1 Senbaru, Nishihara, Okinawa 903-0213, Japan

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Other Title
  • シトクロム<i>c</i>の多量体形成に関する理論的研究

Abstract

<p>Cytochrome c is a hemoprotein that plays an important role in electron transport in the mitochondrial respiratory chain. Cytochrome c forms oligomers by successive domain swapping, where the C-terminal α helices are replaced by the corresponding helices of other cytochrome c molecules, leading to a loss in the electron transfer function. However, the detailed mechanism of domain swapping of cytochrome c is still unclear. To clarify the mechanism of the oligomerization, we have analyzed the thermodynamic stabilities of the domain-swapped dimer. In this paper, we introduce our recent progress.</p>

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