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

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

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 partic...

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Bibliographic Details
Main Authors: Valentina Peleh, Jan Riemer, Andrew Dancis, Johannes M. Herrmann
Format: Article
Language:English
Published: Shared Science Publishers OG 2015-03-01
Series:Microbial Cell
Subjects:
cysteine oxidation
disulfide bonds
Dre2
Fe-S clusters
Mia40
mitochondria
oxidative protein folding
Online Access:http://microbialcell.com/researcharticles/protein-oxidation-in-the-intermembrane-space-of-mitochondria-is-substrate-specific-rather-than-general-2/
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http://microbialcell.com/researcharticles/protein-oxidation-in-the-intermembrane-space-of-mitochondria-is-substrate-specific-rather-than-general-2/

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