Abstract
Employing peptide-based models of copper transporter 1 (CTR1), we show that the trimeric arrangement of its N-terminus tunes its reactivity with Cu, promoting Cu(ii) reduction and stabilizing Cu(i). Hence, the employed multimeric models of CTR1 provide an important contribution to studies on early steps of Cu uptake by cells.
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CITATION STYLE
APA
Galler, T., Lebrun, V., Raibaut, L., Faller, P., & Wezynfeld, N. E. (2020). How trimerization of CTR1 N-terminal model peptides tunes Cu-binding and redox-chemistry. Chemical Communications, 56(81), 12194–12197. https://doi.org/10.1039/d0cc04693k
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