CRCU

Chemical Research in Chinese Universities ›› 2003, Vol. 19 ›› Issue (3): 335-339.

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Catalytical Activities of Reconstructed Hemoglobin with Different Central Ions in Prosthetic Group

LIU Jian-yu1,2, SUN Bao-wei1, LI Yuan-zong1, CHANG Wen-bao1   

  1. 1. Key Lab of Bioorganic Chemistry and Molecular Engineering, Department of Chemical Biology, College of Chemistry and Molecular Engineering, Peking University, Beijing 100871, P. R. China;
    2. Department of Applied Chemistry, South China University of Technology, Guangzhou 510640, P. R. China
  • Received:2002-06-26 Online:2003-08-24 Published:2011-08-06
  • Supported by:

    Supported by the Trans-Century Talent Foundation, the Ministry of Education.

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Abstract: 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.

Key words: Hemoglobin, Reconstruction, Metal displacement, Catalase, Peroxidase