dithiol

Another reported application is the synthesis of macrocycles via dithiol coupling.

The net result is the covalent interconversion of a disulfide and a dithiol.

This colorless, intensely odorous liquid is the simplest chiral dithiol.

RNR gains electrons on the active-site dithiol groups necessary for its activity.

Following a single reduction, RNR requires electrons donated from the dithiol groups of the protein thioredoxin.

The enzyme ferredoxin-thioredoxin reductase uses reduced ferredoxin to reduce thioredoxin from the disulfide form to the dithiol.

Research in the former Soviet Union led to the introduction of DMPS, another dithiol, as a mercury-chelating agent.

In the 1960s, BAL was modified into DMSA, a related dithiol with far fewer side effects.

An example is the dithiol 1,4-Benzenedimethanethiol (SHCHCHCHSH)).

(2S)-2-amino-1,4-dimercaptobutane (dithiobutylamine or DTBA) is a new dithiol reducing agent that somewhat overcomes this limitation of DTT.

Thus, the two substrates of this enzyme are glutathione and protein disulfide, whereas its two products are glutathione disulfide and protein dithiol.

The active site consists of the active dithiol groups from the RNR1 as well as the diferric center and the tyrosyl radical from the RNR2 subunit.

Finally, the reduced thioredoxin is used to reduced a cysteine-cysteine disulfide bond in SBPase to a dithiol, which converts the SBPase into its active form.

The reduced (that is, dithiol) form of PDI is able to catalyse a reduction of mispaired thiol residues of a particular substrate, acting as an isomerase.

It also includes members of the thioredoxin superfamily with three thioredoxins, two thioredoxin-like proteins, a dithiol and three monocysteine glutaredoxins and a redox-active plasmoredoxin being encoded in the genome.

Special attention is essential in some cases, such as that of dithiol SAMs to avoid problems due to oxidation or photoinduced processes, which can affect terminal groups and lead to disorder and multilayer formation.

The active site of thioredoxin consists of two neighboring cysteines, as part of a highly conserved CXXC motif, that can cycle between an active dithiol form (reduced) and an oxidized disulfide form.

Two cysteines were introduced into the beta barrel structure of the GFP, the oxidation state (reduced dithiol or the oxidized disulfide) of the engineered thiols determines the fluorescence properties of the sensor.

The biologically active form of oxytocin, commonly measured by RIA and/or HPLC techniques, is also known as the octapeptide "oxytocin disulfide" (oxidized form), but oxytocin also exists as a reduced dithiol nonapeptide called oxytoceine.

Another selenium-containing enzyme in some plants and in animals (thioredoxin reductase) generates reduced thioredoxin, a dithiol that serves as an electron source for peroxidases and also the important reducing enzyme ribonucleotide reductase that makes DNA precursors from RNA precursors.