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Yeast alcohol dehydrogenase catalyzed reduction of p-nitroso-N, N-dimethylaniline by NADH.

The Italian journal of biochemistry (1996-03-01)
V Leskovac, S Trivic, B M Anderson
ABSTRACT

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.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
N,N-Dimethyl-p-phenylenediamine sulfate salt, 98%
Sigma-Aldrich
N,N-Dimethyl-p-phenylenediamine, 97%
Sigma-Aldrich
N,N-Dimethyl-1,4-phenylenediamine oxalate, 98%
Supelco
N,N-Dimethyl-p-phenylenediamine, for spectrophotometric det. of SO42-, S2-, ≥97.0%
Millipore
N,N-Dimethyl-p-phenylenediamine dihydrochloride, suitable for microbiology, ≥99.0%
Sigma-Aldrich
N,N-Dimethyl-p-phenylenediamine dihydrochloride, suitable for peroxidase test, ≥99.0% (titration)