38246-95-6Relevant articles and documents
The involvement of the mitochondrial amidoxime reducing component (MARC) in the reductive metabolism of hydroxamic acidsS
Ginsel, Carsten,Plitzko, Birte,Froriep, Danilo,Stolfa, Diana A.,Jung, Manfred,Kubitza, Christian,Scheidig, Axel J.,Havemeyer, Antje,Clement, Bernd
, p. 1396 - 1402 (2018/09/13)
The mitochondrial amidoxime reducing component is a recently discovered molybdenum enzyme in mammals which, in concert with the electron transport proteins cytochrome b5 and NADH cytochrome b5 reductase, catalyzes the reduction of N-oxygenated structures.
Mechanism and reactivity in perborate oxidation of anilines in acetic acid
Karunakaran, Chockalingam,Kamalam, Ramasamy
, p. 2011 - 2018 (2007/10/03)
Perborate but not percarbonate in acetic acid generates peracetic acid on standing and the peracetic acid oxidation of anilines is fast. The oxidation with a fresh solution of perborate in acetic acid is smooth and second order but the specific oxidation rate increases with increasing [perborate]0 or [boric acid]. Perborate on dissolution affords hydrogen peroxide and a borate; the latter assists the former in the oxidation. The oxidation rates of anilines under identical conditions do not conform to any of the linear free energy relationships but the reaction rates of molecular anilines do. Perborate oxidation proceeds via two reaction paths but the overall oxidation rates of molecular anilines conform to structure reactivity relationships; the transition states do not differ significantly. Analysis of the oxidation rates of perborate and percarbonate reveals that while perborate oxidation is faster than percarbonate it is at least as selective as the latter.
Kinetics and Mechanism of Oxidation of para-Substituted Anilines by Peroxomonosulphate
Abdul Jameel,Maruthamuthu
, p. 368 - 370 (2007/10/03)
Kinetics of oxidation of several para-substituted anilines by peroxomonosulphate (PMS) in aqueous acetic acid medium have been investigated. The reaction follows a total second order, first order each in [PMS] and [substrate]. The reaction rate is retarted by both electron-releasing and withdrawing groups. Absence of free radical formation is confirmed. Activation energy and thermodynamic parameters have been computed. A probable mechanism has been proposed.
Synthesis of N-arylhydroxylamines by antimony-catalyzed reduction of nitroarenes
Ren, Pingda,Dong, Tingwei,Wu, Shihui
, p. 1547 - 1552 (2007/10/03)
Metallic antimony catalyzes the reduction of aromatic nitro compounds to the corresponding N-arylhydroxylamines in good yields with NaBH4 under mild conditions. The azoxybenzenes from autoxidation of N-arylhydroxylamines were also obtained in basic conditions.
A Fast Procedure for the Reduction of Azides and Nitro Compounds Based on the Reducing Ability of Sn(SR)3-Species
Bartra, Marti,Romea, Pedro,Urpi, Felix,Vilarrasa, Jaume
, p. 587 - 594 (2007/10/02)
Tin(II) complexes prepared by treatment of SnCl2 or Sn(SR)2 with appropriate amounts of RSH and Et3N appear to be the best reducing agents for azides (to amines) reported so far.Thes tin(II) complexes also reduce primary and secondary aliphatic nitro compounds to oximes, usually within minutes at r.t. or hours in cold, and tertiary aliphaic as well as aromatic nitro compounds to afford the corresponding hydroxylamines.In general, azides react more rapidly than nitro substituents, whereas carbonyl groups, sulphoxides, sulphones, nitriles, and esters are practically unreactive under the same conditions.Some mechanistic details of the reaction of Sn(SPh)3- with azides and nitro compounds have also been elucidated.
Acid-Catalyzed Hydrolysis of N-Hydroxyacetanilides: Amide Hydrolysis vs N-O Bond Heterolysis
Novak, Michael,Bonham, Gayl A.,Mohler, Linda K.,Peet, Kristine M.
, p. 3903 - 3908 (2007/10/02)
Although it has been widely assumed that N-hydroxy-N-aryl amides decompose in acidic solution by acid-catalyzed N-O bond heterolysis, we have found that the N-hydroxyacetanilides 1a-e largely decompose by the alternative amide hydrolysis pathway.The immediate products of hydrolysis, the hydroxylamines 2a-e, can be detected by direct or indirect methods, but these materials also decompose via the Bamberger rearrangement under the reaction conditions.Only the p-EtO- and p-MeO-substituted N-hydroxyacetanilides (1a and 1b) exhibit any sign of N-O bond heterolysis, and only as a minor component (ca. 7percent) of the overall hydrolysis.No change in mechanism could be found for 1d in H2SO4 solutions as concentrated as 9 M.The lack of reactivity of 1a-e to N-O bond heterolysis is largely due to unfavorable protonation of the OH group.Protonation of the carbonyl oxygen is favored over the hydroxyl oxygen by ca. 7 orders of magnitude.
Mechanism of metabolic activation of the analgetic bucetin to bacterial mutagens by hamster liver microsomes
Nohmi,Ishidate Jr.,Hiratsuka,Watabe
, p. 2877 - 2885 (2007/10/02)
Bucetin (N-(β-hydroxybutyryl)-p-phenetidine) was found to be mutagenic to Salmonella typhimurium TA100 in the presence of liver 9000 g supernatant fractions (S9) prepared from polychlorinated biphenyl (PCB)-treated hamsters and a reduced nicotinamide adenine dinucleotidephosphate (NADPH)-generating system. However, the analgetic was not mutagenic in the presence of NADPH-fortified S9 from PCB-treated rat liver. The mutagenic potency of bucetin was about a quarter of that of the structurally related analgetic, phenacetin. PCB-treated hamster liver microsomes fortified with NADPH activated bucetin to two direct-acting mutagens, N-hydroxy-phenetidine and p-nitrosophenetole, through deacylation followed by N-hydroxylation. The nitroso compound arose from N-hydroxyphenetidine via autoxidation. N-(b-Hydroxybutyryl)-p-amino-phenol, a major metabolite of bucetin under the conditions used, was not mutagenic to TA100 either with or without NADPH-fortified S9 from PCB-treated or untreated rats or hamsters. N-Hydroxybucetin, which was about 70 times less mutagenic than N-hydroxyphenacetin in the presence of PCB-treated hamster S9, was not detected as a metabolite of bucetin from the NADPH-fortified reaction mixtures. Although no species difference was observed in p-phenetidine N-hydroxylation, the rate of bucetin deacylation was over 90 times higher in hamsters than in rats. The rate of microsomal deacylation of bucetin was much lower than that of phenacetin or N-butyryl-p-phenetidine. These results suggest that the species difference in bucetin mutagenicity is due to the difference in deacylating activity between rat and hamster liver microsomes, and also that the β-hydroxyl group in the butyryl side chain makes bucetin poorly hydrolyzable in microsomes, resulting in lower mutagenic activity as compared with phenacetin.
