Deprotection of an N(α)-Fmoc-protected glycocysteine derivative 7 with an excess of morpholine unexpectedly led to the fluorenylmethyl-protected thioether 8 in high yield. The suggested mechanism for this reaction comprises the addition of the cysteine thiolate on the exocyclic double bond of dibenzofulvene, which is formed during Fmoc deprotection. The influence of base concentration on this t...

c-Type cytochromes contain haem covalently attached to protein by thioether bonds formed post-translationally and requiring a dedicated biogenesis apparatus. Three biogenesis systems, found in different cell types, are well known. Here we discuss emerging evidence for at least one additional system, for unanticipated diversity in the location of the systems and for the co-existence of multiple ...

An aryl alkyl thioether, in which the C−S bond is split by a lightning bolt, featured on cover picture illustrating Research Article Mårten Ahlquist, Helena Lundberg et al. (e202304272). The background shows two distinct sections: left showcasing crystalline sulfur and right representing layers of coal. image illustrates use electricity to break bonds for synthetic applications. We thank Dr And...

In order to gain insight into the coordination site and oxidative activity of the CuM site of hydroxylases such as peptidylglycine α-hydroxylating monooxygenase (PHM), dopamine β-monooxygenase (DβM), and tyramine β-monooxygenase (TβM), we have synthesized, characterized and studied the oxidation chemistry of copper complexes chelated by tridentate N2Sthioether, N2Osulfoxide or N2Osulfone donor ...

A tandem 1,3-sulfur migration followed by iodocyclization reaction of propargylic sulfides in the presence NIS HFIP has been developed to synthesize indene-based β-iodoalkenyl sulfides. The choice media is crucial promote reaction. proposed mechanism involving initial activation and favoring sulfur starting thioether via cationic intermediates experimentally supported. In addition, suitability ...

A new metallo-capsule has been synthesised that consists of three copper(II) ions and two molecules of a tris-deprotonated tripodal ligand in which three 2,4-pentanedione groups are linked via their gamma-carbons through thioether spacers to the 1,3,5-positions of a triazine core.

Over the last decade, cysteine thiolate ligands have been shown to be critical to the Cu(I) (cuprous) binding chemistry of many cytosolic metallochaperone and metalloregulatory proteins involved in copper physiology. More recently, the thioether group of methionine has begun to emerge as an important Cu(I) ligand for trafficking proteins in more oxidizing cellular environments.

By utilizing thioether ligands, CuproCleav-1 stabilizes Cu(+) complexes in aqueous solution and releases the guest metal ion upon photolysis of the nitrobenzyl group. The photocage has an apparent K(d) of 54 pM for Cu(+), and metal ion release has been demonstrated using the fluorescent sensor CS1.