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

M.S.T. Koay; B.M.G. Janssen; M. Merkx

doi:10.1039/C2DT32082G

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

M.S.T. Koay, B.M.G. Janssen, M. Merkx

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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.

Original language	English
Pages (from-to)	3230-3232
Number of pages	3
Journal	Dalton Transactions
Volume	42
DOIs	https://doi.org/10.1039/C2DT32082G
Publication status	Published - 2013

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title = "Tuning the metal binding site specificity of a fluorescent sensor protein: from copper to zinc and back",

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.",

author = "M.S.T. Koay and B.M.G. Janssen and M. Merkx",

year = "2013",

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T1 - Tuning the metal binding site specificity of a fluorescent sensor protein: from copper to zinc and back

AU - Koay, M.S.T.

AU - Janssen, B.M.G.

AU - Merkx, M.

PY - 2013

Y1 - 2013

N2 - 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.

AB - 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.

U2 - 10.1039/C2DT32082G

DO - 10.1039/C2DT32082G

M3 - Article

SN - 1477-9226

VL - 42

SP - 3230

EP - 3232

JO - Dalton Transactions

JF - Dalton Transactions

ER -

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

Abstract

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