Hemoglobin(Hb) was de-prosthetized, which was then reconstructed with the prosthetic groups with different central metal ions including Fe(Ⅲ), Co(Ⅱ) and Mn(Ⅱ). The spectral properties along with the catalase and peroxidase activities of the reconstructed hemoglobin were compared with those of Hb and prosthetic groups with different ions. When the central ion is iron, the reconstituted Hb(rHb) has the highest catalase and peroxidase activities. Maybe it is the reason that iron is chosen as the central ion in the prosthetic groups of natural hemoproteins. Different from peroxidase activity, the catalase activity of hemin cannot be enhanced by the microenvironment of apoHb. This result shows that the structure of apoHb is more similar to that of apoHRP than that of apocatalase.