Journal
ACCOUNTS OF CHEMICAL RESEARCH
Volume 38, Issue 10, Pages 775-783Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ar0300118
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Funding
- Biotechnology and Biological Sciences Research Council [P18581] Funding Source: researchfish
- Biotechnology and Biological Sciences Research Council [P18581] Funding Source: Medline
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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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