Protein oxidation in the intermembrane space of mitochondria is substrate-specific rather than general

@inproceedings{Peleh2014ProteinOI,
  title={Protein oxidation in the intermembrane space of mitochondria is substrate-specific rather than general},
  author={Valentina Peleh and Jan Riemer and Andrew Dancis and Johannes M Herrmann},
  booktitle={Microbial cell},
  year={2014}
}
In most cellular compartments cysteine residues are predominantly reduced. However, in the bacterial periplasm, the ER and the mitochondrial intermembrane space (IMS), sulfhydryl oxidases catalyze the formation of disulfide bonds. Nevertheless, many IMS proteins contain reduced cysteines that participate in binding metal- or heme-cofactors. In this study, we addressed the substrate specificity of the mitochondrial protein oxidation machinery. Dre2 is a cysteine-rich protein that is located in… CONTINUE READING

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References

Publications referenced by this paper.
Showing 1-10 of 50 references

Intermembrane Space Proteome of Yeast Mitochondria*

Molecular & cellular proteomics : MCP • 2012
View 1 Excerpt

Dual role of mitofilin in mitochondrial membrane organization and protein biogenesis

K von der Malsburg, JM Muller, +21 authors M van der Laan
Dev. Cell • 2011
View 1 Excerpt

Multiple ways to make disulfides.

Trends in biochemical sciences • 2011
View 1 Excerpt

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