Issue 31, 2018

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

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

Supplementary files

Article information

Article type
Communication
Submitted
03 اپریل 2018
Accepted
11 جوٗلایی 2018
First published
18 جوٗلایی 2018

Dalton Trans., 2018,47, 10443-10446

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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