Further studies on the reaction of disulphides with silver nitrate

Cecil, R.; McPhee, J.R.

doi:10.1042/bj0660538

Cited by 58 publications

(20 citation statements)

References 10 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Stricks & Kolthoff (1951) showed that, with cystine and oxidized glutathione, the equilibrium RS-SR+SO32-= RS S03-+ RS is dependent on pH, as this affects the relative proportions of RS-+ RSH present. Cecil & McPhee (1955) and McPhee (1956) studied the kinetics of the reaction of sulphite with a number of simple disulphides. They observed that under the conditions used reaction took place with S032but not with HS03ions.…”

mentioning

confidence: 99%

“…This is shown by allowing the reaction to reach equilibrium and acidifying to approx. pH 2 (which freezes the equilibrium) before estimating the amount of thiol formed (Cecil & McPhee, 1955). If the titration is carried out at the reaction pH, then removal of thiol from the system (as mercaptide) causes the reaction to 'follow' the titration and go to completion.…”

mentioning

confidence: 99%

See 1 more Smart Citation

The reaction of the disulphide groups of insulin with sodium sulphite

Cecil

Loening

1960

Biochemical Journal

Self Cite

View full text Add to dashboard Cite

mentioning

confidence: 99%

mentioning

confidence: 99%

The reaction of the disulphide groups of insulin with sodium sulphite

Cecil

Loening

1960

Biochemical Journal

Self Cite

View full text Add to dashboard Cite

“…Meanwhile, the disulfide moiety has also been found to react with transition metal ions in several different pathways. For example, disulfides can (i) form simple adducts or coordination complexes and (ii) undergo oxidation S−S bond cleavage reactions from the transition metal . Such oxidative S−S bond cleavage can sometimes involve homolysis of the S−S bond and it is well known that the homolysis step is assisted by high temperatures (>100 °C) .…”

Section: Resultsmentioning

confidence: 99%

Room‐temperature carbon–sulfur bond formation from Ni(II) σ‐aryl complex via cleavage of the S–S bond of disulfide moieties

Housekeeper

Luscombe

2013

Applied Organom Chemis

View full text Add to dashboard Cite

The formation of ArSY (Y: C(= S)NMe 2 , Ph, P(= O)(OEt) 2 ) by reductive elimination from s-aryl complexes (M(PPh 3 ) 2 PhBr, M = Ni, Pd), associated with disulfides (YSÀSY, Y: C(=S)NMe 2 (1), Ph (2), P(=O)(OEt) 2 (3)), at ambient temperature, has been investigated. Various mechanistic features of disulfide bond (SÀS) cleavage have been elucidated using disulfide 1 by 31 P NMR spectroscopy and matrix-assisted laser desorption/ionization-time of flight mass spectrometric investigations. Based upon the results of nucleophilic cleavage of the SÀS bond by PPh 3 , studies of the reductive elimination process show that when M(PPh 3 ) 2 PhBr is mixed with disulfide 1, competitive reactions occur between the PPh 3 ligand, disulfide 1 and a trace amount of water, leading to low CÀS coupling yields; an oxidation reaction of PPh 3 with disulfide and water occur prior to CÀS cross-coupling, and phosphonium ion intermediates are likely involved. However, when the disulfide 1 is pretreated with PPh 3 , the Ni(II) s-aryl complex affords the CÀS coupling product nearly quantitatively at room temperature. The pretreatment method is also effective for the coupling reaction of disulfide 2 and Ni(II) s-aryl complex. The difference between Ni(II) and Pd (II) s-aryl complexes on CÀS bond formation by reductive elimination can be explained by the affinity of metal for the thiolate ligands derived from the cleaved disulfide.

show abstract

“…Cecil and McPhee [6] postulated the irreversible binding of silver to cystine according to the following scheme:…”

Section: Discussionmentioning

confidence: 99%

Histochemical localization of high-sulfur keratins with silver nitrate

Wagner

Giesen

Zahn

1983

Colloid & Polymer Sci

View full text Add to dashboard Cite

Abstract:The treatment of merino wool with ammoniacal silver nitrate results in a selective staining of high-sulfur proteins. The method has been applied to unmodified and reduced fibres. The electron microscopical studies are supplemented by a quantitative analysis by means of atomic absorption spectrophotometry. At the saturation point no difference in the silver uptake of reduced and unreduced fibres can be established. However, the samples show considerable differences regarding the kinetics of the reaction. The photometric analysis yields a silver uptake of 3 mol Ag/mol cysteine and 6 mol Ag/mol cystine. The silver deposition depends upon the formation of silver mercaptide and silver complexes of unknown structure. In comparison with cysteine the mercaptide formation from cystine occurs very slowly, because the disulfide bond first has to be cleaved.

show abstract

Further studies on the reaction of disulphides with silver nitrate

Cited by 58 publications

References 10 publications

The reaction of the disulphide groups of insulin with sodium sulphite

The reaction of the disulphide groups of insulin with sodium sulphite

Room‐temperature carbon–sulfur bond formation from Ni(II) σ‐aryl complex via cleavage of the S–S bond of disulfide moieties

Histochemical localization of high-sulfur keratins with silver nitrate

Contact Info

Product

Resources

About