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19F NMR investigations of cobalt(II) complexes with cysteine-containing peptide ligands

✍ Scribed by Wei-Yin Sun; Takafumi Ueno; Norikazu Ueyama; Akira Nakamura


Publisher
John Wiley and Sons
Year
1995
Tongue
English
Weight
395 KB
Volume
33
Category
Article
ISSN
0749-1581

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✦ Synopsis


Abstract

Isotropically shifted ^19^F NMR signals were observed for novel mononuclear Co(II) complexes, (Et~4~N)~2~[Co(Z‐Cys‐Pro‐Leu‐Cys‐Gly‐X)~2~] (Z = benzyloxycarbonyl, X = NHC~6~H~4~‐p = F, NHC~6~H~4~‐m‐F and NHCH~2~CH~2~C~6~H~4~‐p‐F). Such isotropically shifted signals show very short ^19^F spin‐lattice relaxation times (T~1~) in the range 20–150 ms compared with the corresponding SH‐free peptide ligands, Z‐Cys(SH)‐Pro‐Leu‐Cys(SH)‐Gly‐X, which revealed signals with ^19^F T~1~ values in the range 1600–3200 ms. The observed ^19^F NMR isotropic shifts and short ^19^F T~1~ values in the Co(II)‐cysteine‐peptide complexes are ascribed to the formation of NH—S hydrogen bonds and the presence of interactions of aromatic groups with the sulphur atom of the coordinated cysteine residue.


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