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The Role of Histidine in a Copper‐Specific Metallothionein
Author(s) -
PérezRafael Sílvia,
Pagani Ayelen,
Palacios Òscar,
Dallinger Reinhard,
Capdevila Mercè,
Atrian Sílvia
Publication year - 2013
Publication title -
zeitschrift für anorganische und allgemeine chemie
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.354
H-Index - 66
eISSN - 1521-3749
pISSN - 0044-2313
DOI - 10.1002/zaac.201300053
Subject(s) - helix pomatia , metallothionein , histidine , mutant , copper , residue (chemistry) , biochemistry , gene isoform , snail , chemistry , alanine , recombinant dna , amino acid residue , amino acid , microbiology and biotechnology , biology , peptide sequence , ecology , gene , organic chemistry
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 Cu I 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.
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