81576-12-7Relevant articles and documents
Hydroxamic Acid Production and Active-site Induced Bamberger Rearrangement from the Action of α-Ketoglutarate Dehydrogenase on 4-Chloronitrosobensene
Corbett, Michael D.,Corbett, Bernadette R.,Doerge, Daniel R.
, p. 345 - 350 (2007/10/02)
THe α-ketoglutarate dehydrogenase complex obtained from E. coli has been found to convert 4-chloronitrosobenzene (3) into N-(4-chlorophenyl)succinohydroxamic acid (4) and N-(4-chloro-2-hydroxyphenyl)succinamic acid (5).The conversion of 4-chloronitrosobenzene (3) into these two products is not quantitative and attempts to identify other, significant low-molecular-weight metabolites have been unsuccessful.Partial enzyme-inactivation has been observed during the incubation of 4-chloronitrosobensene (3) with α-ketoglutarate dehydrogenase.The direct enzymic conversion of the hydroxamic acid (4) into the isomeric product (5) did not occur.These results are interpreted on the basis of a mechanism in which N-(4-chlorophenyl)hydroxylamine (6) is generated at the enzyme active-site by a redox process.Condensation of the active-site bound products would give rise to the hydroxamic acid (4) directly, while a Bamberger-like rearrangement of the active-site bound hydroxylamine(6), followed by condensation of the resulting o-aminophenol, would explain the production of the succinamic acid.
