The role of histidine in a copper-specific metallothionein

Sílvia Pérez-Rafael, Ayelen Pagani, Òscar Palacios, Reinhard Dallinger, Mercè Capdevila, Sílvia Atrian

Research output: Contribution to journalArticleResearchpeer-review

6 Citations (Scopus)


Metallothioneins achieve metal binding specificity by modulation of their amino acid sequences through evolution. Non-coordinating residues seem to play a key role in this function, and among them histidine may be of particular importance. Here we report how this residue regulates CuI binding to a highly copper specific isoform, the CuMT of the snail Helix pomatia, by analysis of the recombinant complexes yielded by a constructed mutant where this residue has been changed to an alanine. Copyright © 2013 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Original languageEnglish
Pages (from-to)1356-1360
JournalZeitschrift fur Anorganische und Allgemeine Chemie
Issue number8-9
Publication statusPublished - 1 Jul 2013


  • Copper
  • Cu-thionein
  • Helix pomatia
  • Histidine
  • Metallothioneins


Dive into the research topics of 'The role of histidine in a copper-specific metallothionein'. Together they form a unique fingerprint.

Cite this