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Issue 9, 2013
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Tuning the metal binding site specificity of a fluorescent sensor protein: from copper to zinc and back

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Abstract

We previously reported the development of high affinity Zn2+ FRET sensors based on the Zn2+-mediated interaction between the CXXC motifs present in the copper chaperone proteins ATOX1 and WD4. By systematically substituting several of these cysteines for methionines, we constructed sensor variants that retain a high affinity for Cu+, while effectively abolishing their ability to form stable tetrahedral Zn2+ complexes.

Graphical abstract: Tuning the metal binding site specificity of a fluorescent sensor protein: from copper to zinc and back

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Publication details

The article was received on 09 Sep 2012, accepted on 04 Oct 2012 and first published on 04 Oct 2012


Article type: Communication
DOI: 10.1039/C2DT32082G
Citation: Dalton Trans., 2013,42, 3230-3232
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    Tuning the metal binding site specificity of a fluorescent sensor protein: from copper to zinc and back

    M. S. Koay, B. M. G. Janssen and M. Merkx, Dalton Trans., 2013, 42, 3230
    DOI: 10.1039/C2DT32082G

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