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

5 Citations (Scopus)

Abstract

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
Volume639
Issue number8-9
DOIs
Publication statusPublished - 1 Jul 2013

Keywords

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

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