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Issue 31, 2018
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Stabilizing intramolecular cobalt–imidazole coordination with a remote methyl group in the backbone of a cofactor B12–protein model

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Abstract

This communication describes the stabilizing effect (ΔΔG° = −4 kJ mol−1) of a remote methyl group in the backbone of a cobalamin–enzyme mimic on intramolecular imidazole–cobalt coordination. For this purpose, two B12 derivatives with an appended imidazole base were synthesized and analysed with spectrophotometric pH titrations. Qualitative conformation analysis of the backbone structure suggests that a thermodynamically unfavoured gauche interaction in the base-off form of a model containing an (R)-configured CH3 group at position C176 of the linker between the corrin ring and the terminal imidazole ligand steers the base toward cobalt coordination.

Graphical abstract: Stabilizing intramolecular cobalt–imidazole coordination with a remote methyl group in the backbone of a cofactor B12–protein model

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Publication details

The article was received on 03 Apr 2018, accepted on 11 Jul 2018 and first published on 18 Jul 2018


Article type: Communication
DOI: 10.1039/C8DT01298A
Citation: Dalton Trans., 2018,47, 10443-10446
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    Stabilizing intramolecular cobalt–imidazole coordination with a remote methyl group in the backbone of a cofactor B12–protein model

    M. Sonnay and F. Zelder, Dalton Trans., 2018, 47, 10443
    DOI: 10.1039/C8DT01298A

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