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. 2014 Dec 12;426(24):4087-4098.
doi: 10.1016/j.jmb.2014.10.022. Epub 2014 Nov 1.

"VSports手机版" Mia40 combines thiol oxidase and disulfide isomerase activity to efficiently catalyze oxidative folding in mitochondria

Johanna R Koch  1 , Franz X Schmid  2
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Mia40 combines thiol oxidase and disulfide isomerase activity to efficiently catalyze oxidative folding in mitochondria (V体育官网入口)

"V体育ios版" Johanna R Koch et al. J Mol Biol. .

Abstract

Mia40 (a mitochondrial import and assembly protein) catalyzes disulfide bond formation in proteins in the mitochondrial intermembrane space. By using Cox17 (a mitochondrial copper-binding protein) as a natural substrate, we discovered that, in the presence of Mia40, the formation of native disulfides is strongly favored. The catalytic mechanism of Mia40 involves a functional interplay between the chaperone site and the catalytic disulfide. Mia40 forms a specific native disulfide in Cox17 much more rapidly than other disulfides, in particular, non-native ones, which originates from the recently described high affinity for hydrophobic regions near target cysteines and the long lifetime of the mixed disulfide VSports手机版. In addition to its thiol oxidase function, Mia40 is active also as a disulfide reductase and isomerase. We found that species with inadvertently formed incorrect disulfides are rebound by Mia40 and reshuffled, revealing a proofreading mechanism that is steered by the conformational folding of the substrate protein. .

Keywords: disulfide relay; mitochondrial disulfide formation; mitochondrial import; mitochondrial intermembrane space; oxidative protein folding V体育安卓版. .

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