Lookup NU author(s): Dr Arnaud Basle,
Professor Christopher Dennison
This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).
© 2017 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim. Bacteria possess cytosolic proteins (Csp3s) capable of binding large quantities of copper and preventing toxicity. Crystal structures of a Csp3 plus increasing amounts of CuI provide atomic-level information about how a storage protein loads with metal ions. Many more sites are occupied than CuI equiv added, with binding by twelve central sites dominating. These can form [Cu4(S-Cys)4] intermediates leading to [Cu4(S-Cys)5]-, [Cu4(S-Cys)6]2-, and [Cu4(S-Cys)5(O-Asn)]- clusters. Construction of the five CuI sites at the opening of the bundle lags behind the main core, and the two least accessible sites at the opposite end of the bundle are occupied last. Facile CuI cluster formation, reminiscent of that for inorganic complexes with organothiolate ligands, is largely avoided in biology but is used by proteins that store copper in the cytosol of prokaryotes and eukaryotes, where this reactivity is also key to toxicity.
Author(s): Basle A, Platsaki S, Dennison C
Publication type: Article
Publication status: Published
Journal: Angewandte Chemie - International Edition
Print publication date: 01/07/2017
Online publication date: 19/06/2017
Acceptance date: 15/05/2017
Date deposited: 28/06/2017
ISSN (print): 1433-7851
ISSN (electronic): 1521-3773
Publisher: Wiley - VCH Verlag
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