Related Experiment Video
Updated: Aug 16, 2026

Defining Substrate Specificities for Lipase and Phospholipase Candidates
Published on: November 23, 2016
Nucleophilic dephosphorylation of p-nitrophenyl diphenyl phosphate in cationic micellar media
Kallol K Ghosh1, Daliya Sinha, Manmohan L Satnami
1School of Studies in Chemistry, Pt. Ravishankar Shukla University, Raipur, 492010 India. kallolkghosh@yahoo.com
Abstract:
The kinetics of nucleophilic dephosphorylation of p-nitrophenyl diphenyl phosphate by hydroxamate ions (R'(C=O)N(RO-)) have been investigated in aqueous cationic micellar media at pH 9.12 and 27 degrees C. The pseudo-first-order rate constant-surfactant profiles show micelle-assisted bimolecular reactions involving interfacial ion exchange between bulk aqueous media and micellar pseudophase. N-Substituted hydroxamate ion shows higher reactivity over the unsubstituted hydroxamate ions in cationic micellar media. The kinetic data are discussed in terms of the pseudophase ion exchange model.
More Related Videos
10:53Anionic Polymerization of an Amphiphilic Copolymer for Preparation of Block Copolymer Micelles Stabilized by π-π Stacking Interactions
Published on: October 10, 2016
09:04Sequence-specific and Selective Recognition of Double-stranded RNAs over Single-stranded RNAs by Chemically Modified Peptide Nucleic Acids
Published on: September 21, 2017
Related Concept Videos
Nucleophiles
Detergent Purification of Membrane Proteins
Predicting Products: SN1 vs. SN2
With increased substitution on the alkyl halide,...
Phosphorylation
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...