Acta Phys. -Chim. Sin. ›› 2010, Vol. 26 ›› Issue (04): 1107-1112.doi: 10.3866/PKU.WHXB20100410

• BIOPHYSICAL CHEMISTRY • Previous Articles     Next Articles

Interaction of Nickel(II) with Yeast Alcohol Dehydrogenase

YIN Guo-Wei, WEI Wei, XU Jia, LI Zhi-Fen, WANG Bao-Huai, DU Wei-Hong   

  1. Depaetment of Chemistry, Renmin University of China, Beijing 100872, P. R. China; Institute of Physical Chemistry, College of Chemistry and Molecular Engineering, Peking University, Beijing 100871, P. R. China
  • Received:2009-10-26 Revised:2009-12-16 Published:2010-04-02
  • Contact: DU Wei-Hong


The binding mode of metal ions with proteins is usually different in different systems. Yeast alcohol dehydrogenase (YADH) is a zinc containing metalloenzyme that catalyzes the fermentation reaction of alcohol to acetaldehyde. UV-Vis spectroscopy, fluorescence spectroscopy, and differential scanning calorimetry (DSC) were used to investigate the interaction of nickel(II) with Yeast alcohol dehydrogenase. The binding of Ni(II) to Yeast alcohol dehydrogenase shows a 320 nm UV absorbance band and the enzyme conformational change is reflected in the fluorescence data. Both UV-Vis and fluorescence spectra exhibit biphasic kinetics for the binding process. The interaction of Ni(II) with Yeast alcohol dehydrogenase causes the enzyme to transform from a tetramer to a dimer. The conformational change of the Yeast alcohol dehydrogenase results in an increase in the denaturation temperature and in a molar enthalpy change during the DSC process. This study reveals a complex but deep-seated mechanism for the interaction of Ni(II) with YADH.

Key words: Conformational change, Nickel(II), Yeast alcohol dehydrogenase, Interaction


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