Journal
INORGANIC CHEMISTRY
Volume 54, Issue 17, Pages 8544-8551Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acs.inorgchem.5b01162
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Funding
- Lilly Endowment, Saint Mary's College, Department of Chemistry Physics
- Center for Academic Innovations at Saint Mary's College
- Maryjean R. Burke and Daughters SISTAR award
- National Science Foundation [CHE-1362662]
- DOE Office of Biological and Environmental Research
- National Institutes of Health, National Center for Research Resources, Biomedical Technology Program [P41RR001209]
- U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences [DE-AC02-98CH10886]
- Case Center for Synchrotron Biosciences through the National Institute of Biomedical Imaging and Bioengineering (NIH) [P30-EB-009998]
- West Grid
- Compute Canada Calcul Canada
- Direct For Mathematical & Physical Scien
- Division Of Chemistry [1152054] Funding Source: National Science Foundation
- Division Of Chemistry
- Direct For Mathematical & Physical Scien [1362662] Funding Source: National Science Foundation
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Copper is a vital metal cofactor in enzymes that are essential to myriad biological processes. Cellular acquisition of copper is primarily accomplished through the Ctr family of plasma membrane copper transport proteins. Model peptide studies indicate that the human Ctr1 N-terminus binds to Cu(II) with high affinity through an amino terminal Cu(II), Ni(II) (ATCUN) binding site. Unlike typical ATCUN-type peptides, the Ctr1 peptide facilitates the ascorbate-dependent reduction of Cu(II) bound in its ATCUN site by virtue of an adjacent HR (his-His) sequence in the peptide. It is likely that the Cu(I) coordination environment influences the redox behavior of Cu bound to this peptide; however, the identity and coordination geometry of the Cu(I) site has not been elucidated from previous work. Here, we show data from NMR, XAS, and structural modeling that sheds light on the identity of the Cu(I) binding site of a Ctr1 model peptide. The Cu(I) site includes the same his-His site identified in previous work to facilitate ascorbate-dependent Cu(II) reduction. The data presented here are consistent with a rational mechanism by which Ctr1 provides coordination environments that facilitate Cu(II) reduction prior to Cu(I) transport.
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