Browse by author
Lookup NU author(s): Dr Stephen Tottey, Dr Duncan Harvie, Professor Nigel Robinson
Full text for this publication is not currently held within this repository. Alternative links are provided below where available.
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. © 2005 American Chemical Society.
Author(s): Tottey S, Harvie DR, Robinson NJ
Publication type: Review
Publication status: Published
Journal: Accounts of Chemical Research
Year: 2005
Volume: 38
Issue: 10
Pages: 775-783
Print publication date: 01/10/2005
ISSN (print): 0001-4842
ISSN (electronic): 1520-4898
URL: http://dx.doi.org/10.1021/ar0300118
DOI: 10.1021/ar0300118
PubMed id: 16231873
