Robust affinity standards for Cu(I) biochemistry.

ABSTRACT: The measurement of reliable Cu(I) protein binding affinities requires competing reference ligands with similar binding strengths; however, the literature on such reference ligands is not only sparse but often conflicting. To address this deficiency, we have created and characterized a series of water-soluble monovalent copper ligands, MCL-1, MCL-2, and MCL-3, that form well-defined, air-stable, and colorless complexes with Cu(I) in aqueous solution. X-ray structural data, electrochemical measurements, and an extensive network of equilibrium titrations showed that all three ligands form discrete Cu(I) complexes with 1:1 stoichiometry and are capable of buffering Cu(I) concentrations between 10(-10) and 10(-17) M. As most Cu(I) protein affinities have been obtained from competition experimen

SUBMITTER: Bagchi P 

PROVIDER: S-EPMC3983694 | biostudies-literature | 2013 Dec

REPOSITORIES: biostudies-literature