The N-terminal soluble domains of Bacillus subtilis CopA exhibit a high affinity and capacity for Cu(i) ions
Author:
Publisher
Royal Society of Chemistry (RSC)
Subject
Inorganic Chemistry
Link
http://pubs.rsc.org/en/content/articlepdf/2009/DT/B810412C
Reference48 articles.
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2. The copBL operon protects Staphylococcus aureus from copper toxicity: CopL is an extracellular membrane–associated copper-binding protein;Journal of Biological Chemistry;2019-03
3. Mass spectrometric studies of Cu(I)-binding to the N-terminal domains of B. subtilis CopA and influence of bacillithiol;Journal of Inorganic Biochemistry;2019-01
4. The N-terminal domains of Bacillus subtilis CopA do not form a stable complex in the absence of their inter-domain linker;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2018-02
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