Mitochondrial disulfide bond formation is driven by intersubunit electron transfer in Erv1 and proofread by glutathione.

@article{Bien2010MitochondrialDB,
  title={Mitochondrial disulfide bond formation is driven by intersubunit electron transfer in Erv1 and proofread by glutathione.},
  author={Melanie Bien and Sebastian Longen and Nikola Wagener and Ilona Chwalla and Johannes M Herrmann and Jan Riemer},
  journal={Molecular cell},
  year={2010},
  volume={37 4},
  pages={516-28}
}
The disulfide relay system in the intermembrane space of mitochondria is of crucial importance for mitochondrial biogenesis. Major players in this pathway are the oxidoreductase Mia40 that oxidizes substrates and the sulfhydryl oxidase Erv1 that reoxidizes Mia40. To analyze in detail the mechanism of this oxidative pathway and the interplay of its components, we reconstituted the complete process in vitro using purified cytochrome c, Erv1, Mia40, and Cox19. Here, we demonstrate that Erv1… CONTINUE READING

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