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Visualizing Biological Copper Storage: The Importance of Thiolate-Coordinated Tetranuclear Clusters

Lookup NU author(s): Dr Arnaud Basle, Semeli Platsaki, 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.

Publication metadata

Author(s): Basle A, Platsaki S, Dennison C

Publication type: Article

Publication status: Published

Journal: Angewandte Chemie - International Edition

Year: 2017

Volume: 56

Issue: 30

Pages: 8697-8700

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


DOI: 10.1002/anie.201703107


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Funder referenceFunder name
BB/K008439/1Biotechnology and Biological Sciences Research Council (BBSRC)