Alternative Conformations of Cytochrome c: Structure, Function, and Detection.

@article{Hannibal2016AlternativeCO,
  title={Alternative Conformations of Cytochrome c: Structure, Function, and Detection.},
  author={Luciana Hannibal and Florencia Tomasina and Daiana A Capdevila and Ver{\'o}nica Demicheli and Ver{\'o}nica T{\'o}rtora and Dami{\'a}n {\'A}lvarez-Paggi and Ronald Jemmerson and Daniel H Murgida and Rafael Radi},
  journal={Biochemistry},
  year={2016},
  volume={55 3},
  pages={407-28}
}
Cytochrome c (cyt c) is a cationic hemoprotein of ∼100 amino acid residues that exhibits exceptional functional versatility. While its primary function is electron transfer in the respiratory chain, cyt c is also recognized as a key component of the intrinsic apoptotic pathway, the mitochondrial oxidative protein folding machinery, and presumably as a redox sensor in the cytosol, along with other reported functions. Transition to alternative conformations and gain-of-peroxidase activity are… CONTINUE READING