[Noncompetitive activation of peroxidase oxidation of o-phenylenediamine by melamine]

Bioorg Khim. 2003 Jan-Feb;29(1):49-56. doi: 10.1023/a:1022278402568.
[Article in Russian]

Abstract

Peroxidase-catalyzed oxidation of o-phenylenediamine (PDA) is greatly activated with melamine (MA) in 15 mM phosphate-citrate buffer at pH 6.0-7.4 in a noncompetitive manner: kcat and Km increase in direct proportion to the MA concentration. An extent of the activation is quantitatively characterized with a coefficient alpha (in M-1), which essentially increases along with the rise in pH from 6.0 to 7.4. MA acts as a nucleophilic catalyst in the oxidation process: it most likely affects the peroxidase active site from the distal position of heme. MA non-competitively inhibits the peroxidase oxidation of PDA at pH 4.3, since it completely loses its nucleophilic properties in acidic medium. A rapid, highly accurate, and simple analytical test system based on the kinetics of melamine-activated oxidation of PDA is proposed for the quantitative determination of melamine within the concentration range of 10(-4)-10(-3) M. This test system uses the spectrophotometric determination of the PDA oxidation product at 455 nm.

Publication types

  • English Abstract

MeSH terms

  • Hydrogen-Ion Concentration
  • Kinetics
  • Oxidation-Reduction
  • Peroxidases / metabolism*
  • Phenylenediamines / metabolism*
  • Triazines / metabolism*

Substances

  • Phenylenediamines
  • Triazines
  • 1,2-diaminobenzene
  • Peroxidases
  • melamine