A kinetic study of the reaction of horseradish peroxidase with hydrogen peroxide.
A kinetic study has been carried out over the pH range of 2.63-9.37 for the reaction of horseradish peroxidase with hydrogen peroxide to form compound I of th;e enzyme. Analysis of the results, indicates that there are two kinetic influencing, ionizable groups on the enzyme with pKa values of 3.2 and 3.9. Protonation of these groups results in a decrease in the rate of reaction of the enzyme with H2O2. A previous study of the kinetics of cyanide binding to horseradish peroxidase (Ellis, W.D. & Dunford, H.B.: Biochemistry 7, 2054-2062 (1968)) has been extended to down to pH 2.55, and analysis of these results also indicates the presence of two kinetically important ionizable groups on the enzyme with pKa values of 2.9 and 3.9.
D002021:Buffers; D003486:Cyanides / Q000378:metabolism; D006861:Hydrogen Peroxide / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008433:Mathematics; D008956:Models, Chemical; D010544:Peroxidases / Q000378:metabolism*; D010944:Plants / Q000201:enzymology*; D011485:Protein Binding; D013053:Spectrophotometry
D002021:Buffers; D003486:Cyanides; D006861:Hydrogen Peroxide; D010544:Peroxidases