Participation of Low Molecular Weight Electron Carriers in Oxidative Protein Folding

International Journal of Molecular Sciences

Éva Margittai¹  Miklós Csala¹  József Mandl¹ 

[1] Department of Medical Chemistry, Molecular Biology and Pathobiochemistry, Semmelweis University & MTA-SE Pathobiochemistry Research Group, 1444 Budapest, POB 260, Hungary

关键词: Oxidative folding;    ascorbate;    tocopherol;    vitamin K;    protein disulfide isomerase;    Ero1;    endoplasmic reticulum;    glutathione;    small-molecule catalysts;   

DOI  :  10.3390/ijms10031346

来源: mdpi

【 摘 要 】

Oxidative protein folding is mediated by a proteinaceous electron relay system, in which the concerted action of protein disulfide isomerase and Ero1 delivers the electrons from thiol groups to the final acceptor. Oxygen appears to be the final oxidant in aerobic living organisms, although the existence of alternative electron acceptors, e.g. fumarate or nitrate, cannot be excluded. Whilst the protein components of the system are well-known, less attention has been turned to the role of low molecular weight electron carriers in the process. The function of ascorbate, tocopherol and vitamin K has been raised recently. In vitro and in vivo evidence suggests that these redox-active compounds can contribute to the functioning of oxidative folding. This review focuses on the participation of small molecular weight redox compounds in oxidative protein folding.

【 授权许可】

CC BY   
© 2009 by the authors; licensee Molecular Diversity Preservation International, Basel, Switzerland. This article is an open-access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).