Hemoglobin was used as a substitute of peroxidase in the catalytic oxidation of P-cresol by H_2O_2. The peroxidative characteristics of hemoglobin and enzymatic kinetics were studied. The K_m value (1.85× 10~(-3)mol·L_(-1)) and V_m value (1.6 min_(-1)) were measured by steady-state catalytic velocity at pH=10.3 and temperature 25℃. The reaction mechanism was discussed when p-cresol was used as a hydrogen donor for hemoglobin. The velocity equation has been obtained. The results indicate that the catalytic activity of hemoglobin is higher tan those of other mimic enzymes (e.g. Hemin, β-CD-Hemin).

Key words: PEROXIDASE, HEMOGLOBIN, ENZYME, CHARACTERISTICS, FLUORESCENCE, HYDROGEN PEROXIDE, METHYL GROUP, PHENAL P, CATALYSIS, DYNAMICS