Peer-Reviewed Publication
J Inorg Biochem2026;282113339.September 1, 2026Journal Article
Cu(I) and Cu(II) binding by hyperactive variants of the human CTR1 N-terminus: Insights from cellular and model peptide studies.
Kaylee Ruth1, Emily Post1, Xiaobin Wu2, Heejeong Kim3, M Jake Pushie4, Maria Escobedo5, Kristin Kuter5, Jaekwon Lee3, Kathryn L Haas6
1Department of Chemistry, Duke University, Durham, NC 27708, USA.
2Redox Biology Center, Department of Biochemistry, University of Nebraska, Lincoln, NE 68588-0664, USA; Development Center of Plant Germplasm Resources, College of Life Sciences, Shanghai Normal University, Shanghai 200234, China.
3Redox Biology Center, Department of Biochemistry, University of Nebraska, Lincoln, NE 68588-0664, USA.
4Department of Surgery, University of Saskatchewan, Saskatoon, SK S7N 5E5, Canada.
5Department of Mathematics and Computer Science, Saint Mary's College, Notre Dame, IN 46556, USA.
6Department of Chemistry, Duke University, Durham, NC 27708, USA. Electronic address: kathryn.haas@duke.edu.
Abstract
Copper (Cu) trafficking requires precise control of Cu(II)/Cu(I) redox chemistry to enable cellular acquisition while preventing toxicity. Human Cu transporter 1 protein (hCTR1) mediates cellular Cu uptake, yet key molecular details governing its extracellular Cu acquisition remain unresolved. Although hCTR1 is a Cu(I)-selective pore, extracellular Cu may be presented by carriers in the Cu(II) oxi…
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