ArticleJournal of the American Chemical Society2013
Robust affinity standards for Cu(I) biochemistry.
Article in Journal of the American Chemical Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 85 citations in OpenAlex.
- TPEN, a Well-Known Zinc Chelator, Sequesters Attomolar-Buffered Cellular Cu(I) Through an Oxygen-Dependent Mechanism.ACS chemical neuroscience · 2026Article
- Activity-based sensing reveals elevated labile copper promotes liver aging via hepatic ALDH1A1 depletion.Nature communications · 2025Article
- Biomimetic Pseudopeptides to Decipher the Interplay between Cu and Methionine-Rich Domains in Proteins.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Cysteine Rich Intestinal Protein 2 is a copper-responsive regulator of skeletal muscle differentiation and metal homeostasis.PLoS genetics · 2024Article
- Methionine-rich domains emerge as facilitators of copper recruitment in detoxification systems.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Selective removal of copper from complex biological media with an agarose-immobilized high-affinity PSP ligand.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024Article
- Cysteine Rich Intestinal Protein 2 is a copper-responsive regulator of skeletal muscle differentiation.bioRxiv : the preprint server for biology · 2024Article
- Copper regulates the host innate immune response against bacterial infection via activation of ALPK1 kinase.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Determination ofSensors (Basel, Switzerland) · 2024Article
- Coordination Chemistry of Sulfur-Containing Bifunctional Chelators: TowardInorganic chemistry · 2023Article
- Pentadentate and Hexadentate Pyridinophane Ligands Support Reversible Cu(II)/Cu(I) Redox Couples.Inorganics · 2023Article
- Important Structural Features of Thiolate-Rich Four-Helix Bundles for Cu(I) Uptake and Removal.Inorganic chemistry · 2023Article
- Conformationally Preorganized High-Affinity Ligands for Copper Biology with Hinged and Rigid Thiophene Backbones.Inorganic chemistry · 2023Article
- Unique underlying principles shaping copper homeostasis networks.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2022Review
- Ionophore Ability of Carnosine and Its Trehalose Conjugate Assists Copper Signal in Triggering Brain-Derived Neurotrophic Factor and Vascular Endothelial Growth Factor Activation In Vitro.International journal of molecular sciences · 2021Article
- Acquisition of ionic copper by the bacterial outer membrane protein OprC through a novel binding site.PLoS biology · 2021Article
- Novel Bifunctional [16]aneSMolecules (Basel, Switzerland) · 2021Article
- Principles and practice of determining metal-protein affinities.The Biochemical journal · 2021Review
- Article
- Preorganized PSP Ligands Yield Monomeric Cu(I) Complexes with Subzeptomolar Cu(I) Dissociation Constants.Inorganic chemistry · 2019Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
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 experiments with bathocuproine disulfonate or 2,2'-bicinchoninic acid, we further calibrated their Cu(I) stability constants against the MCL series. To demonstrate the application of these reagents, we determined the Cu(I) binding affinity of CusF (log K = 14.3 ± 0.1), a periplasmic metalloprotein required for the detoxification of elevated copper levels in Escherichia coli . Altogether, this interconnected set of affinity standards establishes a reliable foundation that will facilitate the precise determination of Cu(I) binding affinities of proteins and small-molecule ligands.
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