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A place for thioether chemistry in cellular copper ion recognition and trafficking

Nature Chemical Biology volume 4, pages 148–151 (2008)Cite this article

Abstract

Over the last decade, cysteine thiolate ligands have been shown to be critical to the Cu(I) (cuprous) binding chemistry of many cytosolic metallochaperone and metalloregulatory proteins involved in copper physiology. More recently, the thioether group of methionine has begun to emerge as an important Cu(I) ligand for trafficking proteins in more oxidizing cellular environments.

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Figure 1: Four crystallographically characterized small-molecule complexes are shown (gray, C; dark yellow, S; red, O; bronze, Cu), labeled with the copper oxidation state.
Figure 2: Characterized Cu(I) trafficking and sensing coordination sites classified by cellular localization and function.

Rebecca Henretta

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Acknowledgements

This research was supported by US National Institutes of Health grant GM 38784 (to T.V.O.) a nd by National Research Service Award GM 071129 (to A.V.D.)

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  1. Anna V. Davis is in the Department of Chemistry and Thomas V. O'Halloran is in the Departments of Chemistry and Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, Illinois 60208, USA. t-ohalloran@northwestern.edu,

    Anna V Davis & Thomas V O'Halloran

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  1. Anna V Davis
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Davis, A., O'Halloran, T. A place for thioether chemistry in cellular copper ion recognition and trafficking. Nat Chem Biol 4, 148–151 (2008). https://doi.org/10.1038/nchembio0308-148

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