[Peroxidase activity of catalase with respect to aromatic amines].
The catalase dissociation into subunits has been studied at pH less than 3.5 and greater than 11.0. This process is characterized by pseudo-first order rate constants, depending on the initial concentrations of the enzyme and H+. At pH 2.85, the steady-state kinetics of five aromatic amines oxidation by catalase monomers has been studied for orthodianisidine (o-DA), 3,5,3',5'-tetramethylbenzidine (TMB), ortho- and para-phenylene diamine (p-PDA) and 5-aminosalycilic acid. The optimal substrates for catalase in acidic solutions are o-DA, TMB and p-PDA. A comparison has been carried out for the catalase peroxidative activity, and the catalytic characteristics of horseradish peroxidase in the oxidation of the same substrate. The mechanisms of peroxidatic amines oxidation by catalase and horseradish peroxidase are discussed.
Artemchik
V D
VD
Kurchenko
V P
VP
Metelitsa
D I
DI
D000588:Amines / Q000378:metabolism*; D000636:Aminosalicylic Acids / Q000378:metabolism; D000818:Animals; D001560:Benzidines / Q000378:metabolism; D002374:Catalase / Q000494:pharmacology*; D002417:Cattle; D066298:In Vitro Techniques; D007527:Isoenzymes; D007700:Kinetics; D008099:Liver / Q000201:enzymology; D010084:Oxidation-Reduction; D009195:Peroxidase; D010544:Peroxidases; D010655:Phenylenediamines / Q000378:metabolism
D000588:Amines; D000636:Aminosalicylic Acids; D001560:Benzidines; D007527:Isoenzymes; D010655:Phenylenediamines; D010544:Peroxidases; D002374:Catalase; D009195:Peroxidase
Peroksidaznaia aktivnost' katalazy po otnosheniiu k aromaticheskim aminam.