Oxidative protein folding in the mitochondrial intermembrane space

Sideris, D.P. and Tokatlidis, K. (2010) Oxidative protein folding in the mitochondrial intermembrane space. Antioxidants and Redox Signaling, 13(8), pp. 1189-1204. (doi:10.1089/ars.2010.3157)

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Disulfide bond formation is a crucial step for oxidative folding and necessary for the acquisition of a protein's native conformation. Introduction of disulfide bonds is catalyzed in specialized subcellular compartments and requires the coordinated action of specific enzymes. The intermembrane space of mitochondria has recently been found to harbor a dedicated machinery that promotes the oxidative folding of substrate proteins by shuttling disulfide bonds. The newly identified oxidative pathway consists of the redox-regulated receptor Mia40 and the sulfhydryl oxidase Erv1. Proteins destined to the intermembrane space are trapped by a disulfide relay mechanism that involves an electron cascade from the incoming substrate to Mia40, then on to Erv1, and finally to molecular oxygen via cytochrome c. This thiol–disulfide exchange mechanism is essential for the import and for maintaining the structural stability of the incoming precursors. In this review we describe the mechanistic parameters that define the interaction and oxidation of the substrate proteins in light of the recent publications in the mitochondrial oxidative folding field.

Item Type:Articles
Glasgow Author(s) Enlighten ID:Tokatlidis, Professor Kostas
Authors: Sideris, D.P., and Tokatlidis, K.
College/School:College of Medical Veterinary and Life Sciences > Institute of Molecular Cell and Systems Biology
Journal Name:Antioxidants and Redox Signaling
Publisher:Mary Ann Liebert, Inc.
ISSN (Online):1557-7716
Copyright Holders:Copyright © 2010 Mary Ann Liebert, Inc.
First Published:First published in Antioxidants and Redox Signaling 13(8):1189-1204
Publisher Policy:Reproduced in accordance with the copyright policy of the publisher

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