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Cu(I) coordination by two plant metallothioneins

Type of publication Peer-reviewed
Publikationsform Original article (peer-reviewed)
Publication date 2013
Author Wan X., Schicht O., Freisinger E.,
Project A. Structures and properties of plant metallothioneins and related artificial proteins - B. Site specific modifications of larger nucleic acids
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Original article (peer-reviewed)

Journal Z. Anorg. Allg. Chem.
Volume (Issue) 639
Page(s) 1365 - 1369
Title of proceedings Z. Anorg. Allg. Chem.
DOI 10.1002/zaac.201300096


The plant metallothioneins (MTs) show high sequence diversity. Proposed to function mainly in metal ion homeostasis and detoxification these small cysteine-rich proteins exhibit pronounced affinities to metal ions with the electron configuration d10. Having previously studied the coordination abilities of two MTs from Cicer arietinum (chickpea) for divalent metal ions we now aim to expand the knowledge to the binding characteristics for CuI. Performing titration studies followed by UV and circular dichroism spectroscopy distinct differences between the two proteins are revealed.