CzcE from Cupriavidus metallidurans CH34 is a copper-binding protein

被引：26

作者：

Zoropogui, Anthony ^{[1
]}

Gambarelli, Serge ^{[2
]}

Coves, Jacques ^{[1
]}

机构：

[1] CNRS CEA UJF, Inst Biol Struct Jean Pierre Ebel, Lab Prot Membranaires, UNR 5075, F-38027 Grenoble, France

[2] CEA, UMR E3 CEA UJF, Dept Rech Fondamentale,Lab Resonance Magnet, Mat Condensee Serv Chim Inorgan & Biol, F-38054 Grenoble 9, France

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2008年 / 365卷 / 04期

关键词：

heavy metal resistance; copper; zinc; metal binding protein; czc determinant; cupriavidus metallidurans CH34;

D O I：

10.1016/j.bbrc.2007.11.030

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

CzcE is encoded by the most distal gene of the czc determinant that allows Cupriavidus metallidurans CH34 to modulate its internal concentrations of cobalt, zinc and cadmium by regulation of the expression of the efflux pump CzcCBA. We have overproduced and purified CzcE. CzcE is a periplasm-located dimeric protein able to bind specifically 4 Cu-equivalent per dimer. Spectrophotometry and EPR are indicative of type 11 copper with typical d-d transitions. Re-oxidation of fully reduced CzcE led to the formation of an air stable semi-reduced form binding both 2 Cu(I) and 2 Cu(II) ions. The spectroscopic characteristics of the semi-reduced form are different of those of the oxidized one, suggesting a change in the environment of Cu(II). (c) 2007 Elsevier Inc. All rights reserved.

引用

页码：735 / 739

页数：5

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