Nucleophilic cleavage of diaryl disulphides

Happer, D. A. R.; Mitchell, J. W.; Wright, G. J.

doi:10.1071/ch9730121

Cited by 16 publications

(4 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Such behavior would be expected for the least reactive, that is least electrophilic, disulfides. From other studies, this result would be expected for disulfides substituted with electron-donating substituents. ,− In the present case, however, quite the opposite behavior is observed, and such a deactivated disulfide 3a still shows clean second-order behavior in the thiolate−disulfide exchange reaction. Saturation behavior with respect to the disulfide concentration would be expected if the first step were rate-determining.…”

Section: Resultssupporting

confidence: 79%

See 1 more Smart Citation

Zinc-Bound Thiolate−Disulfide Exchange: A Strategy for Inhibiting Metallo-β-lactamases

Boerzel

Koeckert

et al. 2003

Inorg. Chem.

View full text Add to dashboard Cite

The mononuclear zinc thiolate complexes [(Tp(PhMe))Zn(S-R)], where Tp(PhMe) is hydrotris((3-methyl-5-phenyl)pyrazolyl)borate and (S-R) is benzyl thiolate, 4-nitrophenylthiolate, 4-trifluoromethylphenylthiolate, 4-chlorophenylthiolate, phenylthiolate, 2-methylphenylthiolate, 4-methylphenylthiolate, 4-methoxyphenylthiolate, or 4-hydroxyphenylthiolate, were synthesized. Representative members of the class were also characterized structurally. The benzyl thiolate complex undergoes a thiolate-disulfide exchange reaction with a variety of diphenyl and dipyridyl disulfides. Kinetic studies revealed that the reaction shows saturation behavior in both complex and disulfide for most of the disulfides studied. Combined with studies of the lability of the coordinated thiolate, a mechanism is proposed where the reactive species is the zinc-coordinated thiolate. When the free benzyl thiol was allowed to react with the same disulfides, the reaction was slower by a factor of 20-200 than that for the zinc-thiolate complex, depending on the particular disulfide employed. Since most metallo-beta-lactamases contain one or more cysteine residues, the one in the active site being coordinated to zinc, the present study was extended to examine whether disulfides can be used as inhibitors of these enzymes by selective oxidation of the metal-bound cysteine. Several disulfides allowed to react with metallo-beta-lactamase CcrA from Bacteroides fragilis were moderate to potent irreversible inhibitors of the enzyme.

show abstract

Section: Resultssupporting

confidence: 79%

“…Reductive cleavage of this compound would produce a thiolate more basic than benzenethiolate or the corresponding zinc complex. Such behavior would be contrary to a trend seen in the reaction of nucleophiles with disulfides, where the most acidic thiolate is the one preferentially liberated …”

Section: Resultscontrasting

confidence: 61%

Zinc-Bound Thiolate−Disulfide Exchange: A Strategy for Inhibiting Metallo-β-lactamases

Boerzel

Koeckert

et al. 2003

Inorg. Chem.

View full text Add to dashboard Cite

show abstract

“…Ethyl-4-carbomethoxyphenyl Disulfide (5). The analytical (and kinetic) sample was purified by Kugelrohr distillation (oven temperature 118-124°, 0.03 Torr): vmax (film) 1704,1269, and 1099 cm-1; NMR (CCL) 1.8-2.7 (A2B2 pattern, 4 H, ArH), 6.12 (s, 3 H, OCHa), 7.26 (q, J = 7 Hz, 2 H, CH2), and 8.70 (t, J = 7 Hz, 3 H, CH3).…”

Section: Resultsmentioning

confidence: 99%

Nucleophilic cleavage of the sulfur-sulfur bond by phosphorus nucleophiles. III. Kinetic study of the reduction of a series of ethyl aryl disulfides with triphenylphosphine and water

Overman¹,

PETTY²

1975

J. Org. Chem.

View full text Add to dashboard Cite

show abstract

“…The first mechanistic hypothesis is the S N 2 synchronous process characterized by the nucleophile and the leaving group acting at the same time in the transition state [192]. Alternatively, one can postulate an addition-elimination mechanism, in which a three-center intermediate is identified with both entering and leaving group bonded to the central chalcogen [193,194] (Scheme 22).…”

Section: Nucleophilic Attack Of a Thiol/thiolate Anion At Diselenidesmentioning

confidence: 99%

Organodiselenides: Organic Catalysis and Drug Design Learning from Glutathione Peroxidase

Tiezza¹,

Ribaudo

Orian³

2019

COC

View full text Add to dashboard Cite

Organodiselenides are an important class of compounds characterized by the presence of two adjacent covalently bonded selenium nuclei. Among them, diaryldiselenides and their parent compound diphenyl diselenide attract continuing interest in chemistry as well as in close disciplines like medicinal chemistry, pharmacology and biochemistry. A search in SCOPUS database has revealed that in the last three years 105 papers have been published on the archetypal diphenyl diselenide and its use in organic catalysis and drug tests. The reactivity of the Se-Se bond and the redox properties of selenium make diselenides efficient catalysts for numerous organic reactions, such as Bayer- Villiger oxidations of aldehydes/ketones, epoxidations of alkenes, oxidations of alcohols and nitrogen containing compounds. In addition, organodiselenides might find application as mimics of glutathione peroxidase (GPx), a family of enzymes, which, besides performing other functions, regulate the peroxide tone in the cells and control the oxidative stress level. In this review, the essential synthetic and reactivity aspects of organoselenides are collected and rationalized using the results of accurate computational studies, which have been carried out mainly in the last two decades. The results obtained in silico provide a clear explanation of the anti-oxidant activity of organodiselenides and more in general of their ability to reduce hydroperoxides. At the same time, they are useful to gain insight into some aspects of the enzymatic activity of the GPx, inspiring novel elements for rational catalyst and drug design.

show abstract

Nucleophilic cleavage of diaryl disulphides

Cited by 16 publications

References 0 publications

Zinc-Bound Thiolate−Disulfide Exchange: A Strategy for Inhibiting Metallo-β-lactamases

Zinc-Bound Thiolate−Disulfide Exchange: A Strategy for Inhibiting Metallo-β-lactamases

Nucleophilic cleavage of the sulfur-sulfur bond by phosphorus nucleophiles. III. Kinetic study of the reduction of a series of ethyl aryl disulfides with triphenylphosphine and water

Organodiselenides: Organic Catalysis and Drug Design Learning from Glutathione Peroxidase

Contact Info

Product

Resources

About