Cytochrome c polymerization by successive domain swapping at the C-terminal helix.

@article{Hirota2010CytochromeCP,
  title={Cytochrome c polymerization by successive domain swapping at the C-terminal helix.},
  author={Shun Hirota and Yoko Hattori and Satoshi Nagao and M Taketa and Hirofumi Komori and Hironari Kamikubo and Zhonghua Wang and Isao Takahashi and Shigeru Negi and Yukio Sugiura and Mikio Kataoka and Yoshiki Higuchi},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2010},
  volume={107 29},
  pages={12854-9}
}
Cytochrome c (cyt c) is a stable protein that functions in a monomeric state as an electron donor for cytochrome c oxidase. It is also released to the cytosol when permeabilization of the mitochondrial outer membrane occurs at the early stage of apoptosis. For nearly half a century, it has been known that cyt c forms polymers, but the polymerization mechanism remains unknown. We found that cyt c forms polymers by successive domain swapping, where the C-terminal helix is displaced from its… CONTINUE READING