Short oligopeptides with three cysteine residues as models of sulphur-rich Cu(i)- and Hg(ii)-binding sites in proteins-Reference-Cited by-同舟云学术

Short oligopeptides with three cysteine residues as models of sulphur-rich Cu(i)- and Hg(ii)-binding sites in proteins

Published:2018 Issue:9 Volume:10 Page:1232-1244
ISSN:1756-5901
Container-title:Metallomics
language:en
Short-container-title:Metallomics

Author:

Mesterházy Edit¹²³⁴⁵,Lebrun Colette⁶⁷⁸⁹,Crouzy Serge¹⁰²³¹¹⁴,Jancsó Attila⁶⁷⁸⁹^ORCID,Delangle Pascale¹²³⁴⁵^ORCID

Affiliation:

1. INAC/SYMMES/Université Grenoble Alpes

2. CEA

3. CNRS

4. 38000 Grenoble

5. France

6. Department of Inorganic and Analytical Chemistry

7. University of Szeged

8. Szeged H-6720

9. Hungary

10. BIG/LCBM/Université Grenoble Alpes

11. (UMR 5249)

Abstract

Peptides mimicking sulphur-rich fragments found in metallothioneins display unexpectedly different behaviours with the two metal ions Hg(ii) and Cu(i).

Funder

Fondation pour la Recherche Médicale

Agence Nationale de la Recherche

Campus France

Nemzeti Kutatási, Fejlesztési és Innovációs Hivatal

Publisher

Oxford University Press (OUP)

Subject

Metals and Alloys,Biochemistry,Biomaterials,Biophysics,Chemistry (miscellaneous)

Link

http://pubs.rsc.org/en/content/articlepdf/2018/MT/C8MT00113H

Reference83 articles.

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4. Crystal structure of the Atx1 metallochaperone protein at 1.02 Å resolution

5. Optical and TDPAC spectroscopy of Hg(II)-rubredoxin: model for a mononuclear tetrahedral [Hg(CysS)4]2− center

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