Artículos de revistas
The role of histidine in a copper-specific metallothionein
Fecha
2013-03Registro en:
Perez Rafael, Silvia; Pagani, María Ayelén; Palacios, Oscar Martín; Dallinger, Reinhard; Capdevila, Merce; et al.; The role of histidine in a copper-specific metallothionein; Wiley; Zeitschrift Fur Anorganische Und Allgemeine Chemie; 639; 8-9; 3-2013; 1356-1360
0044-2313
Autor
Perez Rafael, Silvia
Pagani, María Ayelén
Palacios, Oscar Martín
Dallinger, Reinhard
Capdevila, Merce
Atrian, Silvia
Resumen
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.