Chem. J. Chinese Universities ›› 2009, Vol. 30 ›› Issue (11): 2139.

• Articles • Previous Articles     Next Articles

Methanol-induced Conformation Change of Myoglobin in Basic Solution

JIANG Dan1, CHU Yan-Qiu1, CHEN Nan-Sheng1,2, DING Chuan-Fan1*   

  1. 1. Shanghai Key Laboratory of Molecular Catalysis and Innovative materials, Laser Chemistry Institute, Department of Chemistry, Fudan University, Shanghai 200433, China;
    2. Department of Molecular Biology and Biochemistry, Simon Fraser University, Canada
  • Received:2009-07-07 Online:2009-11-10 Published:2009-11-10
  • Contact: DING Chuan-Fan. E-mail: cfding@fudan.ac.cn
  • Supported by:

    国家自然科学基金(批准号: 25027004)资助.

Abstract:

This paper reports the methanol-induced conformation change of myoglobin in basic solution. According to the results of mass spectrometry, we found that the conformation of myoglobin(Mb) changed in different volume fractions of methanol at pH=11.0, 11.4, 12.0. And both of the methanol concentration and pH value have some effect. Mb exists as hMb at pH=11.0, aMb at pH=12.0, aMb at pH=11.4 except in 30% volume fraction of methanol solution. Using negative ion mass spectrometry mode, Mb all show mainly as aMb. More information of Fe ion′s coordination and electron spin state were found via CD spectrometry and UV-Vis Soret absorption.

Key words: Protein; Molecular conformation; Electrospray ionization-mass spectrometry; Myoglobin; Basic solution

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