Chemical Research in Chinese Universities ›› 2011, Vol. 27 ›› Issue (3): 450-454.

• Articles • Previous Articles     Next Articles

Structure Characteristic and Catalase Activity of Vitreoscilla Hemoglobin Bound with Membrane

ZHAO Hai-feng1, WU Lei1, LU Ming1, HU Yu-lin2, HAN Xiao1 and LI Zheng-qiang1*   

  1. 1. Key Laboratory for Molecular Enzymology & Engineering, Ministry of Education, Jilin University, Changchun 130012, P. R. China;
    2. Medical Department of Liver Gall Pancreas, the First Hospital of Jilin University, Changchun 130021, P. R. China
  • Received:2011-01-06 Revised:2011-02-22 Online:2011-05-25 Published:2011-04-29
  • Contact: LI Zheng-qiang E-mail:lzq@jlu.edu.cn
  • Supported by:

    Supported by the National Natural Science Foundation of China(No.30670458).

Abstract: Lipid-bound [VHb(406)] and lipid-free [VHb(402)] wide type Vitreoscilla hemoglobin were separated from E. coli BL21(DE3). The RZ is 3.30 for [VHb(406)] and 3.15 for [VHb(402)], respectively. VHb(406) shows a characteristic absorption band at 626 nm, while VHb(402) shows one at 644 nm, and it has more α-helix than VHb(402). Data of Raman spectra experiment shows under the excitation wavelength 488 nm, υ4 vibration of both VHb(402) and VHb(406) had a pure and strong signal at 1375 cm-1, which proves that iron porphyrin of both the samples is at their trivalence oxidation state. And no matter lipid binds VHb or not, the vinyl of porphyrin is at cis state. The catalase activity of Vitreoscilla hemoglobin was explored with L-dopa and H2O2 as substrates. The results indicate that VHb(406) has more catalase activity than VHb(402), VHb is a cell’s oxygen modulator and its catalase ability is modulated by the membrane.

Key words: Vitreoscilla hemoglobin, Structure, Function, Membrane binding