Transmembrane electron transfer by the membrane DsbD occurs via a disulfide bond cascade

Article Abstract:

Research demonstrates the ability of the cytoplasmic membrane protein DsbD to mediate electron transfer from the cytoplasm to the periplasm in Escherichia coli. Data point out that the transfer involves interactions between thioredoxin and DsbD and periplasmic substrates.

Escherichia coli, Membrane proteins, Oxidation-reduction reaction, Oxidation-reduction reactions, Electron transport

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Bridge over troubled waters: sensing stress by disulfide bond formation

Article Abstract:

Previous studies have established that disulfide bond formation has the capability to regulate protein activity. In addition, some experiments found evidences that prove that disulfide bond formation may also be a consequence of cellular stress. This has been particularly observed in experiments with eukaryotic cells where it was seen that disulfide bonds are created in response to oxidative stress.

Chemical bonds, Mechanical chemistry, Mechanochemistry, Disulfiram

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Electron Avenue: pathways of disulfide bond formation and isomerization

Article Abstract:

Pathways of disulfide bond isomerization and formation are discussed in this review article. The mechanism elaborated by cells for oxidation of cysteine residues is extremely intricate compared to that earlier thought to exist and to the uncomplicated primary reaction. Topics discussed include folding of proteins involving covalent links between pairs of cysteines to form disulfide bonds, eukaryotes/prokaryotes and electron movements in both disulfide bond formation and protein disulfide bond isomerization.

Statistical Data Included, Prokaryotes, Cytochemistry, Protein folding, Chemistry, Physical and theoretical, Physical chemistry, Isomerization, Catalysis, Cysteine

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