75531-71-4Relevant academic research and scientific papers
Reaction of N-acetyl- and N-[1-(arylsulfonylimino)ethyl]-1,4-benzoquinone imines with sodium arenesulfinates
Konovalova,Avdeenko,Pirozhenko,Ledeneva,Santalova
, p. 1283 - 1291 (2015/01/09)
N-Acetyl- and N-[1-(arylsulfonylimino)ethyl]-1,4-benzoquinone imines having no substituent in the 2- and/or 6-position of the quinoid ring react with sodium arenesulfinates preferentially according to the 1,4-addition pattern. The presence of an ArSO
Rat liver microsomal cytochrome P450-dependent oxidation of 3,5-disubstituted analogues of paracetamol
Bessems,Te Koppele,Van Dijk,Van Stee,Commandeur,Vermeulen
, p. 647 - 666 (2007/10/03)
1. The cytochrome P450-dependent binding of paracetamol and a series of 3,5-disubstituted paracetamol analogues (R = -F, -Cl, -Br, -I, -C(H)3, -C2H5, -iC3H7) have been determined with β-naphthoflavone (βNF)-induced rat liver microsomes and produced reverse type I spectral changes. K(s,app) varied from 0.14 mM for 3,5-diiC3H7-paracetamol to 2.8 mM for paracetamol. 2. All seven analogues underwent rat liver microsomal cytochrome P450-dependent oxidation, as reflected by the formation of GSSG in the presence of GSH. The GSSG-formation was increased in all cases upon pretreatment of rats by β-naphthoflavone (βNF) and was generally decreased upon pretreatment by phenobarbital (PB). 3. Rat liver microsomal cytochrome P450 as well as horseradish peroxidase catalysed the formation of 3,5-disubstituted NAPQI analogues from the corresponding parent compounds, as identified by UV-spectrophotometry of the NAPQI analogues and by GC/MS detection of the following GSH-conjugates: 2-glutathione-S-yl-3,5-dimethyl-1,4-dihydroxybenzene, 2-glutathione-S-yl-3,5-dichloro-paracetamol, and 2-glutathione-S-yl-3,5-dibromo-paracetamol. 4. In liver microsomal (βNF-induced) incubations, apparent K(m) values, as determined for the cytochrome P450 catalysis-dependent oxidation of GSH, for seven 3,5-disubstituted paracetamol analogues (R = -F, -Cl, -Br, -I, -CH3, -C2H5, iC3H7) varied from 0.07 to 0.64 mM. Paracetamol exhibited an apparent K(m) of 0.73 mM. Apparent V(max) values for the cytochrome P450 catalysis dependent oxidation of GSH varied from 0.66 nmol min-1 mg-1 protein for paracetamol to 3.0 nmol min-1 mg-1 protein for 3,5-dimethyl-paracetamol.
NATURE OF THE EFFECT OT THE SUBSTITUENT AT THE NITROGEN ATOM ON THE OXIDATION-REDUCTION POTENTIALS OF p-BENZOQUINONE MONOIMINES
Burmistrov, K. S.,Burmistrov, S. I.
, p. 1279 - 1284 (2007/10/02)
A series of N-acyl-substituted p-benzoquinone monoimines were synthesized.Their oxidation-reduction potentials were investigated, and were correlated with the ? constants and pKa values of the corresponding substituted benzoic acids.A conclusio
