Yeast alcohol dehydrogenase catalyzed reduction of p-nitroso-N, N-dimethylaniline by NADH.
The steady-state kinetics, product identification, stoichiometries, and solvent isotope effects of yeast alcohol dehydrogenase catalyzed reduction of p-nitroso-N,N-dimethylaniline (NDMA) by NADH, are reported. NDMA is enzymatically reduced to p-hydroxylamine-N,N-dimethylaniline, which is further enzymatically dehydrated to corresponding quinonediimine cation (QDI+). QDI+ undergoes nonenzymatic transformations. QDI+ is rapidly reduced by NADH to p-amino-N,N-dimethylaniline (ADMA). Also, QDI+ is readily dismutated with ADMA to form N,N-dimethyl-p-phenylenediamine radicals; radicals are stable under steady-state conditions, below pH 7.5. A complete kinetic mechanism for above reactions has been proposed.
Leskovac
V
V
Faculty of Technology, Novi Sad, Yugoslavia.
Trivic
S
S
Anderson
B M
BM
D000426:Alcohol Dehydrogenase / Q000737:chemistry*; D005609:Free Radicals / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D009243:NAD / Q000737:chemistry*; D009603:Nitroso Compounds / Q000737:chemistry*; D010084:Oxidation-Reduction; D010655:Phenylenediamines / Q000737:chemistry
D005609:Free Radicals; D009603:Nitroso Compounds; D010655:Phenylenediamines; D009243:NAD; C008651:4-nitrosodimethylaniline; C004781:dimethyl-4-phenylenediamine; D000426:Alcohol Dehydrogenase