Protein disulphide bonds are formed in the endoplasmic reticulum of eukaryotic cells and
the periplasmic space of prokaryotic cells. The main pathways that catalyse the formation of …

▪ Abstract Disulfide bonds formed between pairs of cysteines are important features of the
structure of many proteins. Elaborate electron transfer pathways have evolved Escherichia …

Many cellular functions involve cysteine chemistry via thiol–disulfide exchange pathways.
The nucleophilic cysteines of the enzymes involved are activated as thiolate. A thiolate is …

The molecular mechanisms underlying thiol-based redox control are poorly defined.
Disulfide bonds between Cys residues are commonly thought to confer extra rigidity and …

The identification of protein disulfide isomerase, almost 50 years ago, opened the way to the
study of oxidative protein folding. Oxidative protein folding refers to the composite process …

Determining the mechanism by which proteins attain their native structure is an important but
difficult problem in basic biology. The study of protein folding is difficult because it involves …

Disulfide bond formation is a catalyzed process in vivo. In prokaryotes, the oxidation of
cysteine pairs is achieved by the transfer of disulfides from the highly oxidizing DsbA/DsbB …

Disulfide bond formation is required for the correct folding of many secreted proteins. Cells
possess protein-folding catalysts to ensure that the correct pairs of cysteine residues are …

Significance: The discovery of the oxidoreductase disulfide bond protein A (DsbA) in 1991
opened the way to the unraveling of the pathways of disulfide bond formation in the …

Disulfide-bond formation is important for the correct folding of a great number of proteins that
are exported to the cell envelope of bacteria. Bacterial cells have evolved elaborate systems …