Copper Delivery by Metallochaperone Proteins
Abstract
Copper is an essential element in all living organisms, serving as a cofactor for many important proteins and enzymes. Metallochaperone proteins deliver copper ions to specific physiological partners by direct protein-protein interactions. The Atx1-like chaperones transfer copper to intracellular copper transporters, and the CCS chaperones shuttle copper to copper,zinc superoxide dismutase. Crystallographic studies of these two copper chaperone families have provided insights into metal binding and target recognition by metallochaperones and have led to detailed molecular models for the copper transfer mechanism.
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Copper trafficking often involves bis-coordination of Cu+ ions by two thiolate groups with a transient addition of a third thiolate.
“Like Hg2+, copper trafficking often involves bis-coordination of Cu+ ions by two thiolate groups with a transient addition of a third thiolate.211”
From Metals in Motion: Understanding Labile Metal Pools in Bacteria (2025) · cites this paper as [211]
The thiolate coordination chemistry of Hg2+ provides a model for how Hg2+ can transfer between resistance proteins MerT, MerR, and MerA and foreshadowed the similar pathway for Cu+ transfer between chaperones and client proteins.
“This provides a model for how Hg2+ can transfer between resistance proteins that function in transport (MerT), sensing (MerR), and reduction (MerA) and foreshadowed the similar pathway described for the transfer of Cu+ between chaperones and client proteins.196,211”
From Metals in Motion: Understanding Labile Metal Pools in Bacteria (2025) · cites this paper as [211]
Cites
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Dogterom, M., & Yurke, B. (1997) · Science · doi:10.1126/science.278.5339.856 · Cited by 579 · see citing works
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Achila, D., Banci, L., Bertini, I., Bunce, J., Ciofi-Baffoni, S., & Huffman, D. L. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0504472103 · Cited by 169 · see citing works
Serum copper and zinc levels in individuals with autism spectrum disorders
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The Mechanism of Cu+ Transport ATPases
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Metals in Motion: Understanding Labile Metal Pools in Bacteria
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- Authors
- Rosenzweig, A. C.
- Affiliations
- Northwestern University (US)
- Corresponding author
- Rosenzweig, Amy C.
- ORCID
- Rosenzweig, Amy C.
- Venue
- Accounts of Chemical Research
- Publisher
- American Chemical Society (ACS)
- Published
- 2000-12-13
- Volume
- 34
- Issue
- 2
- Pages
- 119-128
- ISSN
- 0001-4842 (ISSN-L)
- 1520-4898
- OpenAlex
- W1994007675
- Cited by
- 279
- References
- 3
- Citations by year
- 2026: 7 · 2025: 8 · 2024: 7 · 2023: 3 · 2022: 5 · 2021: 4 · 2020: 5 · 2019: 4 · 2018: 12 · 2017: 4 · 2016: 6 · 2015: 11 · 2014: 13 · 2013: 7 · 2012: 10
- FWCI
- 16.84
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Accounts of Chemical Research (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Nursing › Nutrition and Dietetics › Trace Elements in Health
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
- Keywords
- copper transport, copper-zinc superoxide dismutase, copper transporters, protein-protein interaction, metal ion binding, target recognition, metal cofactors
- MeSH terms
- Carrier Proteins, Fungal Proteins, Models, Molecular, Protein Binding, Superoxide Dismutase, Molecular Structure, Molecular Chaperones, Saccharomyces cerevisiae Proteins
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