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

Research output: Contribution to journalArticleAcademicpeer-review

17 Citations (Scopus)
1 Downloads (Pure)

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 languageEnglish
Pages (from-to)3230-3232
Number of pages3
JournalDalton Transactions
Volume42
DOIs
Publication statusPublished - 2013

Fingerprint Dive into the research topics of 'Tuning the metal binding site specificity of a fluorescent sensor protein: from copper to zinc and back'. Together they form a unique fingerprint.

  • Cite this