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Zinc Transfer Kinetics of Metallothioneins and Their Fragments with Apo‐carbonic Anhydrase
Author(s) -
Huang ZhongXian,
Liu Fang,
Zheng Qi,
Yu WenHao
Publication year - 2001
Publication title -
chinese journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.28
H-Index - 41
eISSN - 1614-7065
pISSN - 1001-604X
DOI - 10.1002/cjoc.20010190506
Subject(s) - chemistry , zinc , carbonic anhydrase , carbonic anhydrase ii , glutathione , metalloprotein , kinetics , metal , molecule , enzyme , stereochemistry , inorganic chemistry , biochemistry , organic chemistry , physics , quantum mechanics
Abstract The zinc transfer reactions from Zn 7 ‐MT‐I, Zn 7 ‐MT‐II, Zn 4 ‐α fragment (MT‐I) and Zn 4 ,‐α fragment (MT‐II) to apo‐carbonic anhydrase have been studied. In each reaction, no more than one zinc ion per molecule is involved in metal transfer. Zn 7 ‐MT‐I and Zn 7 ‐MT‐II donate zinc to apo‐carbonic anhydrase and de novo constitute it at a comparable efficiency, while Zn 7 ‐MT‐II exhibits a little faster rate. Surprisingly, Zinc is released from Zn 4 ‐α fragment (MT‐II) with a much faster rate than from Zn 4 ‐α fragment (MT‐I), whose rate is close to that of Zn 7 ‐MT‐I. The reason for the difference is still unknown. Introducing complex compounds into this system may give rise to an effect on the reaction. The transfer from Zn 7 ‐MT‐II in the presence of reduced glutathione shows little difference compare to the control, suggesting that the reduced glutathione is not involved in zinc transfer process. However, glutathione disulfide does accelerate this zinc transfer reaction remarkably, indicating that the oxidative factors contribute to zinc release from metallothioneins.