In this Communication, we developed a new procedure for the synthesis of β-hydroxysulfides from thiophenols or diaryl disulfides with TBHP as the oxidant. In the presence of zinc iodide or potassium iodide, with TBHP as the oxidant and pre-reactant, thiophenols and diaryl disulfides reacted with the methyl group of tBuOH smoothly and selectivity to give the corresponding 2-methyl-1-(arylthio)pr...

DsbA and DsbB are responsible for disulfide bond formation. DsbA is the direct donor of disulfides, and DsbB oxidizes DsbA. DsbB has the unique ability to generate disulfides by quinone reduction. It is thought that DsbB oxidizes DsbA via thiol disulfide exchange. In this mechanism, a disulfide is formed across the N-terminal pair of cysteines (Cys-41/Cys-44) in DsbB by quinone reduction. This ...

Upon X-ray irradiation of hypoxic aqueous solution, modified oligodeoxynucleotides (ODNs) bearing a pair of disulfides at both ends of the strand that forms a stem-and-loop structure with a neighboring arrangement of α,ω-bis-disulfides underwent efficient cyclization via an intramolecular exchange reaction at the disulfide moieties with a multiple turnover process. Mechanistic studies revealed ...

The pairing of the 14 half-cystine residues of bovine neurophysin was established by sequential proteolytic digestion. Purified released peptides and the residual disulfide-linked core were monitored at each step by use of amino acid analysis, gas-phase sequencing, and mass spectrometry. The approach included application of gas-phase sequencing to assign disulfide pairs in peptides containing m...

Autotransporters (ATs) are a family of bacterial proteins containing a C-terminal β-barrel-forming domain that facilitates the translocation of N-terminal passenger domain whose functions range from adhesion to proteolysis. Genetic replacement of the native passenger domain with heterologous proteins is an attractive strategy not only for applications such as biocatalysis, live-cell vaccines, a...

We present a convenient and efficient deoxygention method for the syntheses of disulfides thioethers. The reaction involves an iodide-catalyzed reduction methyl sulfinates or sulfoxides, respectively, employing formic acid...

The theoretical self-healing capacity of new sulfenamide-based disulfides is estimated by using theoretical methods of quantum chemistry. Starting from previously studied aromatic disulfides, the influence of inserting a NH group between the disulfide and the phenyl ring (forming the sulfenamide), as well as the role of the phenyl ring in the self-healing process is analyzed. Three parameters a...

Author(s) of this paper may load this reprint on their own web site provided that this cover page is retained. Republication of this article or its storage in electronic databases or the like is not permitted without prior permission in writing from the IUCr. The ability to recognize disulfide bridges automatically in electron density maps would be useful to both protein crystallographers and a...

The formation of disulfides in proteins entering the secretory pathway is catalysed by the protein disulfide isomerase (PDI) family of enzymes. These enzymes catalyse the introduction, reduction and isomerization of disulfides. To function continuously they require an oxidase to reform the disulfide at their active site. To determine how each family member can be recycled to catalyse disulfide ...