Structure and Affinity of Cu(I) Bound to Human Serum Albumin.
| Autor: | Sendzik M; Department of Chemistry and Physics, Saint Mary's College , Notre Dame, Indiana 46556, United States., Pushie MJ; Department of Surgery, University of Saskatchewan , Saskatoon, Saskatchewan S7N 5E5, Canada., Stefaniak E; Department of Chemistry and Physics, Saint Mary's College , Notre Dame, Indiana 46556, United States.; Institute of Biochemistry and Biophysics, Polish Academy of Sciences , Pawińskiego 5a, 02-106 Warsaw, Poland., Haas KL; Department of Chemistry and Physics, Saint Mary's College , Notre Dame, Indiana 46556, United States. |
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| Jazyk: | angličtina |
| Zdroj: | Inorganic chemistry [Inorg Chem] 2017 Dec 18; Vol. 56 (24), pp. 15057-15065. Date of Electronic Publication: 2017 Nov 22. |
| DOI: | 10.1021/acs.inorgchem.7b02397 |
| Abstrakt: | Human serum albumin (HSA) is a major Cu carrier in human blood and in cerebrospinal fluid. A major assumption is that Cu bound to HSA is in the Cu(II) oxidation state; thus, interactions between HSA and Cu(II) have been intensely investigated for over four decades. HSA has been reported previously to support the reduction of Cu(II) to the Cu(I) oxidation state in the presence of the weak reductant, ascorbate; however, the interactions between HSA and Cu(I) have not been explicitly investigated. Here, we characterize both the apparent affinity of HSA for Cu(I) using solution competition experiments and the coordination structure of Cu(I) bound to HSA using X-ray absorption spectroscopy and in silico modeling. We find that HSA binds to Cu(I) at pH 7.4 with an apparent conditional affinity of K |
| Databáze: | MEDLINE |
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