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

International Journal of Molecular Sciences

Hugo Fraga¹ 

[1] Department of Biochemistry and Molecular Biology, Autonomous University of Barcelona, Bellaterra E-08193, Spain

关键词: cysteine motifs;    disulfide bonds;    Erv1;    intermembrane space;    Mia40;    mitochondria;    oxidative protein folding;    protein import;    oxidative stress;   

DOI  :  10.3390/ijms14022916

来源: mdpi

【 摘 要 】

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.

【 授权许可】

CC BY   
© 2013 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland.