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Updated: Jul 19, 2026

Standards for Quantitative Metalloproteomic Analysis Using Size Exclusion ICP-MS
Published on: April 13, 2016
Understanding how cells allocate metals using metal sensors and metallochaperones
Stephen Tottey1, Duncan R Harvie, Nigel J Robinson
1Institute for Cell and Molecular Biosciences, Medical School, University of Newcastle, NE2 4HH, United Kingdom.
Abstract:
Each metalloprotein must somehow acquire the correct metal. We review the insights into metal specificity in cells provided by studies of ArsR-SmtB DNA binding, metal-responsive transcriptional repressors, and a bacterial copper chaperone. Cyanobacteria are the one bacterial group that have known enzymatic demand for cytoplasmic copper import. The copper chaperone and ATPases that supply cyanobacterial plastocyanin and cytochrome oxidase are reviewed, along with related ATPases for cobalt and zinc. These studies highlight the contributions of protein-protein interactions to metal speciation. Metal sensors and metallochaperones, along with metal transporters and metal-storage proteins, act in concert not only to supply the correct metals but also to withhold the wrong ones.
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