Issue 80, 2013
From the journal:

Chemical Communications

Kinetics and thermodynamics of metal binding to the N-terminus of a human copper transporter, hCTR1†

Xiubo Du,ab   Hongyan Li,a   Xinghao Wang,a   Qiong Liu,b   Jiazuan Nib  and  Hongzhe Sun*a  

* Corresponding authors

a Department of Chemistry, The University of Hong Kong, Hong Kong, China
E-mail: hsun@hku.hk
Fax: +852 2857 1586
Tel: +852 2859 8974

b College of Life Sciences, Shenzhen Key Laboratory of Microbial Genetic Engineering, Shenzhen University, Shenzhen 518060, China

Abstract

The N-terminus of hCTR1 was demonstrated to bind three Cu+ ions tightly (log K = 14.92) and reversibly via its Met-rich motifs. Ag+ binds to the protein with the same stoichiometry but much lower affinities than Cu+. The protein also coordinates two Cu2+ ions through its ATCUN motif and His-rich motif with lower affinity. This study provides an insight into the selectivity of the transporter.

Graphical abstract: Kinetics and thermodynamics of metal binding to the N-terminus of a human copper transporter, hCTR1

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Article information

DOI
https://doi.org/10.1039/C3CC45360J
Article type
Communication
Submitted
16 7 2013
Accepted
05 8 2013
First published
07 8 2013

Chem. Commun., 2013,49, 9134-9136

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Kinetics and thermodynamics of metal binding to the N-terminus of a human copper transporter, hCTR1

X. Du, H. Li, X. Wang, Q. Liu, J. Ni and H. Sun, Chem. Commun., 2013, 49, 9134 DOI: 10.1039/C3CC45360J

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