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American Chemical Society, ACS Chemical Biology, 1(9), p. 116-121, 2013

DOI: 10.1021/cb400603t

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Transmembrane Type-2-like Cu^(2+) Site in the P_(1B‑3)-type ATPase CopB: Implications for Metal Selectivity

Journal article published in 2013 by Gabriele Meloni ORCID, Limei Zhang, Douglas C. Rees
This paper is available in a repository.
This paper is available in a repository.

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Abstract

Metal selectivity in P_(1B)-type ATPase transporters is determined by conserved amino acid residues in their transmembrane helices responsible for metal binding and transport across the cellular membrane. The Cu^(2+)-selective CopB from Archaeoglobus fulgidus has been investigated to explore the coordination chemistry of the transition metal binding sites in P_(1B-3)-type ATPases. Electronic absorption, electron paramagnetic resonance, and X-ray absorption spectroscopic studies indicate the presence of a high-affinity transmembrane Type-2-like Cu^(2+) center in which a single cupric ion is coordinated in a distorted square pyramidal geometry by mixed nitrogen/oxygen and sulfur ligands.