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  • 1
    ISSN: 0749-1581
    Keywords: 1H NMR ; Paramagnetic 1H NMR ; Natural abundance 2H NMR ; 19F NMR ; Iron(II) cysteine-peptide complex ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: An Fe(II) complex with Z-Ala-Cys—Pro—Leu—Cys—Gly—NH—C6H4—m—F (Z = benzoxylcarbonyl) having an invariant bidentate peptide ligand, Cys—K—Y—Cys, in rubredoxins was synthesized. The contact-shifted 1H, 2H and 19F NMR signals of (Et4N)2[Fe(Z—Ala—cys—Pro—Leu—cys—Gly—NH—C6H4—m—F)2] (1) in acetonitrile-d3 or acetonitrile at 30°C indicate the existence of two isomers (δ and λ) in the solution of bidentate complex 1 with different orientations of the bidentate peptide ligand to a tetrahedral Fe(II) ion. A novel tetradentate cysteine-containing peptide ligand, cis-1,2-cyclohexylene(CO—Ala—Cys—Pro—Leu—Cys—Gly—NH—C6H4—m—F)2, is designed by energy minimum calculations and synthesized. Its Fe(II) complex, (Et4N)2[Fe(cis-1,2-cyclohexylene(CO-Ala-cys-Pro-Leu-cys-Gly-NH-C6H4-m-F)2)], showed only set of contact-shifted 1H, 2H and 19F NMR signals of Cys CβH2 due to the preferable formation of the δ isomer.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Chichester : Wiley-Blackwell
    Organic Magnetic Resonance 33 (1995), S. 174-177 
    ISSN: 0749-1581
    Keywords: 19F NMR ; isotropic shift ; Co(II)-cysteine-thiolate complexes ; 19F T1 ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Isotropically shifted 19F NMR signals were observed for novel mononuclear Co(II) complexes, (Et4N)2[Co(Z-Cys-Pro-Leu-Cys-Gly-X)2] (Z = benzyloxycarbonyl, X = NHC6H4-p = F, NHC6H4-m-F and NHCH2CH2C6H4-p-F). Such isotropically shifted signals show very short 19F spin-lattice relaxation times (T1) 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 19F T1 values in the range 1600-3200 ms. The observed 19F NMR isotropic shifts and short 19F T1 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.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    Library Location Call Number Volume/Issue/Year Availability
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