Next Article in Journal
Carbapenems to Treat Multidrug and Extensively Drug-Resistant Tuberculosis: A Systematic Review
Next Article in Special Issue
6-Pyrazolylpurine as an Artificial Nucleobase for Metal-Mediated Base Pairing in DNA Duplexes
Previous Article in Journal
Postnatal High-Fat Diet Increases Liver Steatosis and Apoptosis Threatened by Prenatal Dexamethasone through the Oxidative Effect
Previous Article in Special Issue
Ruthenium(III) Complexes of Heterocyclic Tridentate (ONN) Schiff Base: Synthesis, Characterization and its Biological Properties as an Antiradical and Antiproliferative Agent
Article Menu
Issue 3 (March) cover image

Export Article

Open AccessArticle
Int. J. Mol. Sci. 2016, 17(3), 371; doi:10.3390/ijms17030371

Localization and Spectroscopic Analysis of the Cu(I) Binding Site in Wheat Metallothionein Ec-1

Department of Chemistry, University of Zurich, 8057 Zurich, Switzerland
*
Author to whom correspondence should be addressed.
Academic Editor: Kaixun Huang
Received: 22 February 2016 / Revised: 3 March 2016 / Accepted: 7 March 2016 / Published: 11 March 2016
(This article belongs to the Special Issue Applied Bioinorganic Chemistry and Selected Papers from 13th ISABC)
View Full-Text   |   Download PDF [3536 KB, uploaded 11 March 2016]   |  

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). View Full-Text
Keywords: metallothionein; wheat; copper ions; zinc ions; spectroscopy; luminescence spectroscopy metallothionein; wheat; copper ions; zinc ions; spectroscopy; luminescence spectroscopy
Figures

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Supplementary material

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Tarasava, K.; Loebus, J.; Freisinger, E. Localization and Spectroscopic Analysis of the Cu(I) Binding Site in Wheat Metallothionein Ec-1. Int. J. Mol. Sci. 2016, 17, 371.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top