Mia40 Is Optimized for Function in Mitochondrial Oxidative Protein Folding and Import

Mia40 catalyzes oxidative protein folding in mitochondria. It contains a unique catalytic CPC dithiol flanked by a hydrophobic groove, and unlike other oxidoreductases, it forms long-lived mixed disulfides with substrates. We show that this distinctive property originates neither from particular pro...

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Veröffentlicht in:	ACS chemical biology 2014-09, Vol.9 (9), p.2049-2057
Hauptverfasser:	Koch, Johanna R, Schmid, Franz X
Format:	Artikel
Sprache:	eng
Schlagworte:	Catalytic Domain Cation Transport Proteins - chemistry Cation Transport Proteins - metabolism Cysteine - metabolism Disulfides - chemistry Dithionitrobenzoic Acid - chemistry Dithionitrobenzoic Acid - metabolism Escherichia coli Proteins - chemistry Escherichia coli Proteins - metabolism Mitochondrial Membrane Transport Proteins - chemistry Mitochondrial Membrane Transport Proteins - metabolism Models, Molecular Molecular Chaperones - chemistry Molecular Chaperones - metabolism Protein Conformation Protein Disulfide-Isomerases - chemistry Protein Disulfide-Isomerases - metabolism Protein Folding Protein Stability Protein Transport Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - metabolism
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