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The oxidation and reduction of protein disulfide bonds in vitro also generally occurs via thiol–disulfide exchange reactions. Typically, the thiolate of a redox reagent such as glutathione, dithiothreitol attacks the disulfide bond on a protein forming a mixed disulfide bond between the protein and the reagent. This mixed disulfide bond when ...
DTT is a reducing agent; once oxidized, it forms a stable six-membered ring with an internal disulfide bond.It has a redox potential of −0.33 V at pH 7. [1] The reduction of a typical disulfide bond proceeds by two sequential thiol-disulfide exchange reactions and is illustrated below.
Performic acid is a colorless liquid soluble in water, alcohols, ether, benzene, chloroform and other organic solvents. [4] [5] Its strong oxidizing properties are used for cleaving disulfide bonds in protein mapping, [6] as well as for epoxidation, hydroxylation [7] and oxidation reactions in organic synthesis. [5]
2-Mercaptoethanol (also β-mercaptoethanol, BME, 2BME, 2-ME or β-met) is the chemical compound with the formula HOCH 2 CH 2 SH. ME or βME, as it is commonly abbreviated, is used to reduce disulfide bonds and can act as a biological antioxidant by scavenging hydroxyl radicals (amongst others).
Cystine is the disulfide derived from the amino acid cysteine. The conversion can be viewed as an oxidation: 2 HO 2 CCH(NH 2)CH 2 SH + 0.5 O 2 → (HO 2 CCH(NH 2)CH 2 S) 2 + H 2 O. Cystine contains a disulfide bond, two amine groups, and two carboxylic acid groups.
By transferring the disulfide bond between these two cysteine residues onto the folding protein it is responsible for the latter's oxidation. In contrast to bacteria, where the oxidative and isomerization pathways are carried out by different proteins, PDI is also responsible for the reduction and isomerization of the disulfide bonds.
A common 1,4-dithiol is dithiothreitol (DTT), HSCH 2 CH(OH)CH(OH)CH 2 SH, sometimes called Cleland's reagent, for to reduce protein disulfide bonds. Oxidation of DTT results a stable six-membered heterocyclic ring with an internal disulfide bond. Reduction of a typical disulfide bond by DTT via two sequential thiol-disulfide exchange reactions.
TCEP is often used as a reducing agent to break disulfide bonds within and between proteins as a preparatory step for gel electrophoresis.. Compared to the other two most common agents used for this purpose (dithiothreitol and β-mercaptoethanol), TCEP has the advantages of being odorless, a more powerful reducing agent, an irreversible reducing agent (in the sense that TCEP does not ...