65180-94-1Relevant academic research and scientific papers
Kinetic evidence for the occurrence of general acid-base catalysis in N-methylhydroxylaminolysis of N-ethoxycarbonylphthalimide (NCPH)
Khan, M. Niyaz
, p. 647 - 654 (1997)
Pseudo-first-order rate constants (k1 obs) for the reaction of MeNHOH with NCPH obey the relationship: k1 obs = kb' [MeNHOH]T2 where [MeNHOH]T represents total concentration of N-methylhydroxylamine buffer. The rate constants, k1 obs obtained at different total concentration of acetate buffer ([Buf]T] in the presence of 0.004 mol dm-3 MeNHOH follow the relationship: k1 obs = kb[Buf]T. The values of acetate buffer-catalyzed rate constant (kb) at different pH reveal the occurrence of both general base- and general acid- or general base-specific acid-catalysis in the reaction of MeNHOH with NCPH.
Kinetics and mechanism for the formation of o-carboxy(N-methyl)-benzohydroxamic acid in the cleavage of ethyl N-[o-(N-methyl-N-hydroxycarbamoyl)-benzoyl]carbamate in N-methylhydroxylamine, acetate, and phosphate buffers
Khan, M. Niyaz
, p. 427 - 437 (2007/10/03)
The rate of cleavage of ethyl N-[o-(N-methyl-N-hydroxycarbamoyl)benzoyl]-carbamate (ENMBC) in the buffer solutions containing N-methylhydroxylamine, acetate + N-methylhydroxylamine, and phosphate + N-methylhydroxylamine followed an irreversible consecutive reaction path: ENMBC →k 1 obs A →k 2 obs B where A and B represent N-hydroxyl group cyclized product of ENMBC and o-(N-methyl-N-hydroxycarbamoyl)benzoic acid, respectively.
Kinetic Evidence for the Occurrence of Kinetically Detectable Intermediates in the Cleavage of N-Ethoxy-carbonylphthalimide under N-Methylhydroxylamine Buffers
Khan, N. Niyaz
, p. 95 - 103 (2007/10/03)
The kinetics of the aqueous cleavage of N-ethoxycarbonylphthalimide (NCPH) in CH3NHOH buffers of different pH reveals that the cleavage follows the general irreversible consecutive reaction path NCPH(k1obs) -> ENMBC(k2obs) -> A(k3obs) -> B, where ENMBC, A, and B represent ethyl N-[o-(N-methyl-N-hydroxycarbamoyl)benzoyl]carbamate, N-hydroxyl group cyclized product of ENMBC, and o-(N-methyl-N-hydroxycarbamoyl)benzoic acid, respectively. The rate constant k1obs at a constant pH, obeys the relationship k1obs = kw + knapp [Am]T + kb[Am]T2, where [Am]T is the total concentration of CH3NHOH buffer and kw is first-order rate constant for pH-independent hydrolysis of NCPH. Buffer-dependent rate constant kb shows the presence of both general base and general acid catalysis. Both the rate constants k2obs and k3obs are independent of [Am]T (within the [Am]T range of present study) at a constant pH and increase linearly with the increase in αOH with definite intercepts.
