Metal regulation of metallothionein participation in redox reactions

FEBS Letters

Wang, Chih-Chen¹  Zhang, Sen¹  Tsou, Chen-Lu¹  Li, Jian¹ 

[1] National Laboratory of Biomacromolecules, Institute of Biophysics, Academia Sinica, Beijing 100101, China

关键词: Metallothionein;    Redox reaction;    Redox regulation;    Protein disulfide isomerase;    Zinc;    Chelation;    MT;    metallothionein;    GSH;    reduced glutathione;    GSSG;    oxidized glutathione;    RNase A;    ribonuclease A;    PDI;    protein disulfide isomerase;    DTT;    dithiothreitol;    DTNB;    5;    5′-dithiobis-(2-nitrobenzoic acid);   

DOI  :  10.1016/S0014-5793(99)01562-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Like glutathione or dithiothreitol, metallothionein effects the formation of pancreatic ribonuclease A from its S-sulfonated derivative catalyzed by protein disulfide isomerase. EDTA increases the yield of ribonuclease A activity recovery with metallothionein but does not affect the reaction with glutathione or dithiothreitol. EDTA also increases the reactivity of thiol groups in metallothionein with 5,5′-dithiobis-(2-nitrobenzoic acid) by chelation of zinc ions. It is suggested that the thiol groups in metallothionein form a part of the pool of cellular thiols in the regulation of cellular redox reactions and their availability is modulated by zinc chelation.

【 授权许可】

Unknown