Next Article in Journal
Antioxidant, Analgesic, Anti-Inflammatory, and Hepatoprotective Effects of the Ethanol Extract of Mahonia oiwakensis Stem
Next Article in Special Issue
Identification of Oxidative Stress Related Proteins as Biomarkers for Lung Cancer and Chronic Obstructive Pulmonary Disease in Bronchoalveolar Lavage
Previous Article in Journal
Green Approach—Multicomponent Production of Boron—Containing Hantzsch and Biginelli Esters
Previous Article in Special Issue
Disease Progression Mediated by Egr-1 Associated Signaling in Response to Oxidative Stress
Int. J. Mol. Sci. 2013, 14(2), 2916-2927; doi:10.3390/ijms14022916
Review

Oxidative Folding in the Mitochondrial Intermembrane Space in Human Health and Disease

1,*  and 1,2,*
Received: 21 December 2012; in revised form: 21 January 2013 / Accepted: 23 January 2013 / Published: 30 January 2013
(This article belongs to the Special Issue Redox Signaling in Biology and Patho-Biology)
View Full-Text   |   Download PDF [279 KB, uploaded 19 June 2014]   |   Browse Figures
Abstract: Oxidative folding in the mitochondrial intermembrane space (IMS) is a key cellular event associated with the folding and import of a large and still undetermined number of proteins. This process is catalyzed by an oxidoreductase, Mia40 that is able to recognize substrates with apparently little or no homology. Following substrate oxidation, Mia40 is reduced and must be reoxidized by Erv1/Alr1 that consequently transfers the electrons to the mitochondrial respiratory chain. Although our understanding of the physiological relevance of this process is still limited, an increasing number of pathologies are being associated with the impairment of this pathway; especially because oxidative folding is fundamental for several of the proteins involved in defense against oxidative stress. Here we review these aspects and discuss recent findings suggesting that oxidative folding in the IMS is modulated by the redox state of the cell.
Keywords: cysteine motifs; disulfide bonds; Erv1; intermembrane space; Mia40; mitochondria; oxidative protein folding; protein import; oxidative stress cysteine motifs; disulfide bonds; Erv1; intermembrane space; Mia40; mitochondria; oxidative protein folding; protein import; oxidative stress
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Export to BibTeX |
EndNote


MDPI and ACS Style

Fraga, H.; Ventura, S. Oxidative Folding in the Mitochondrial Intermembrane Space in Human Health and Disease. Int. J. Mol. Sci. 2013, 14, 2916-2927.

AMA Style

Fraga H, Ventura S. Oxidative Folding in the Mitochondrial Intermembrane Space in Human Health and Disease. International Journal of Molecular Sciences. 2013; 14(2):2916-2927.

Chicago/Turabian Style

Fraga, Hugo; Ventura, Salvador. 2013. "Oxidative Folding in the Mitochondrial Intermembrane Space in Human Health and Disease." Int. J. Mol. Sci. 14, no. 2: 2916-2927.


Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert