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Oxidative folding in the endoplasmic reticulum: Towards a multiple oxidant hypothesis?
Author(s) -
Margittai Éva,
Bánhegyi Gábor
Publication year - 2010
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2010.05.055
Subject(s) - endoplasmic reticulum , oxidative folding , oxidative phosphorylation , chemistry , biophysics , protein folding , folding (dsp implementation) , stim1 , biochemistry , microbiology and biotechnology , biology , protein disulfide isomerase , electrical engineering , engineering
Oxidative protein folding in the luminal compartment of the endoplasmic reticulum is thought to be mediated by a proteinaceous electron relay system composed by PDI and ER oxidoreductin 1 (Ero1), transferring electrons from the cysteinyl residues of substrate proteins to oxygen. However, recent observations revealed that Ero1 isoforms are dispensable. Endoplasmic reticulum is known as a generator and accumulator of low molecular weight oxidants; some of them have already been shown to promote oxidative folding. On the basis of these observations a new theory of oxidative folding is proposed where the oxidative power is provided by the stochastic contribution of prooxidants.