ArticleInternational journal of molecular sciences2016
Localization and Spectroscopic Analysis of the Cu(I) Binding Site in Wheat Metallothionein Ec-1.
Article in International journal of molecular sciences, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 12 citations in OpenAlex.
- Uncovering the copper(I) binding abilities of a unique fungal metallothionein: characterization ofDalton transactions (Cambridge, England : 2003) · 2026Article
- Small Cysteine-Rich Motif, Big Function─Metal-Driven Dimerization of the CopY C-Terminal Fragment.Inorganic chemistry · 2025Article
- Reaction ofInternational journal of molecular sciences · 2022Article
- Are granulins copper sequestering proteins?Proteins · 2021Article
- Differential reactivity of closely related zinc(II)-binding metallothioneins from the plant Arabidopsis thaliana.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Article
- Metal Substitution and Solvomorphism in Alkylthiolate-Bridged ZnACS omega · 2017Article
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Authors and funding
3 authors at 1 institution in 1 country.
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Abstract
The early cysteine-labeled metallothionein (MT) from Triticum aestivum (common wheat), denoted Ec-1, features two structurally well-defined domains, γ and βE, coordinating two and four Zn(II) ions, respectively. While the protein is currently assumed to function mainly in zinc homeostasis, a low amount of copper ions was also recently detected in a native Ec-1 sample. To evaluate the observed copper binding in more detail, the recombinant Zn₆Ec-1 form was exposed to different amounts of Cu(I) ions and the resulting species characterized with spectroscopic methods. Data reveal that the first Cu(I) equivalent coordinates exclusively to the N-terminal γ-domain of the protein and replaces one Zn(II) ion. To analyze the ability of the γ-domain for coordination of monovalent metal ions in more detail, the γ-Ec-1 peptide fragment was incubated with increasing amounts of Cu(I) and the process monitored with UV-VIS, circular dichroism, and luminescence spectroscopy. Closely similar spectra are observed regardless if the apo- or the metal ion-loaded and, hence, pre-folded forms, were used for the titration experiments with Cu(I). The results indicate that low amounts of Cu(I) ions displace the two metal ions subsequently and stoichiometrically, despite the different coordination geometry requirements of Cu(I) and Zn(II).
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