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Citation: YIN Guo-Wei, WEI Wei, XU Jia, LI Zhi-Fen, WANG Bao-Huai, DU Wei-Hong. Interaction of Nickel(II) with Yeast Alcohol Dehydrogenase[J]. Acta Physico-Chimica Sinica, ;2010, 26(04): 1107-1112. doi: 10.3866/PKU.WHXB20100410 shu

Interaction of Nickel(II) with Yeast Alcohol Dehydrogenase

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 Date: 26 October 2009
Available Online: 8 February 2010

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.
- Conformational change,
- Nickel(II),
- Yeast alcohol dehydrogenase,
- Interaction
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