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Zhou, Liang, Singleton, Chloe and Le Brun, Nick E. 
ORCID: https://orcid.org/0000-0001-9780-4061
(2008)
High Cu(I) and low proton affinities of the CXXC motif of Bacillus subtilis CopZ.
Biochemical Journal, 413 (3).
459–465.
ISSN 0264-6021
Abstract
CopZ, an Atx1-like copper chaperone from the bacterium Bacillus subtilis, functions as part of a complex cellular machinery for Cu(I) trafficking and detoxification, in which it interacts specifically with the transmembrane Cu(I)-transporter CopA. Here we demonstrate that the cysteine residues of the MXCXXC Cu(I)-binding motif of CopZ have low proton affinities, with both exhibiting pKa values of 6 or below. Chelator competition experiments demonstrated that the protein binds Cu(I) with extremely high affinity, with a small but significant pH-dependence over the range pH 6.5–8.0. From these data, a pH-corrected formation constant, ß2=~6×1022 M-2, was determined. Rapid exchange of Cu(I) between CopZ and the Cu(I)-chelator BCS (bathocuproine disulfonate) indicated that the mechanism of exchange does not involve simple dissociation of Cu(I) from CopZ (or BCS), but instead proceeds via the formation of a transient Cu(I)-mediated protein–chelator complex. Such a mechanism has similarities to the Cu(I)-exchange pathway that occurs between components of copper-trafficking pathways.
| Item Type: | Article |
|---|---|
| Faculty \ School: | Faculty of Science > School of Chemistry |
| UEA Research Groups: | Faculty of Science > Research Groups > Biophysical Chemistry (former - to 2017) Faculty of Science > Research Groups > Centre for Ocean and Atmospheric Sciences Faculty of Science > Research Centres > Centre for Molecular and Structural Biochemistry Faculty of Science > Research Groups > Chemistry of Life Processes |
| Depositing User: | Rachel Smith |
| Date Deposited: | 07 Apr 2011 14:16 |
| Last Modified: | 11 Jan 2023 17:33 |
| URI: | https://ueaeprints.uea.ac.uk/id/eprint/28488 |
| DOI: | 10.1042/BJ20080467 |
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