期刊
ZEITSCHRIFT FUR ANORGANISCHE UND ALLGEMEINE CHEMIE
卷 639, 期 8-9, 页码 1356-1360出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/zaac.201300053
关键词
Metallothioneins; Histidine; Cu-thionein; Helix pomatia; Copper
资金
- Spanish Ministerio de Economia y Competitividad [BIO2012-39682-C02-01, BIO2012-39682-C02-02]
- Austrian Science Foundation [P 23635-B20]
- Acciones Integradas (Spain) [HU2006-0027]
- Acciones Integradas (Austria) [ES 02/2007]
- Departament de Quimica, Universitat Autonoma de Barcelona
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.
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