Stabilizing intramolecular cobalt-imidazole coordination with a remote methyl group in the backbone of a cofactor B 12 -protein model

This communication describes the stabilizing effect (ΔΔG° = -4 kJ mol ) of a remote methyl group in the backbone of a cobalamin-enzyme mimic on intramolecular imidazole-cobalt coordination. For this purpose, two B derivatives with an appended imidazole base were synthesized and analysed with spectro...

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Bibliographic Details
Published in:Dalton transactions : an international journal of inorganic chemistry 2018-08, Vol.47 (31), p.10443-10446
Main Authors: Sonnay, Marjorie, Zelder, Felix
Format: Article
Language:English
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Summary:This communication describes the stabilizing effect (ΔΔG° = -4 kJ mol ) of a remote methyl group in the backbone of a cobalamin-enzyme mimic on intramolecular imidazole-cobalt coordination. For this purpose, two B 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 CH group at position C176 of the linker between the corrin ring and the terminal imidazole ligand steers the base toward cobalt coordination.
ISSN:1477-9226
1477-9234
DOI:10.1039/c8dt01298a