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Updated: Feb 7, 2026

Sequence-specific Labeling of Nucleic Acids and Proteins with Methyltransferases and Cofactor Analogues
Published on: November 22, 2014
Stabilizing intramolecular cobalt-imidazole coordination with a remote methyl group in the backbone of a cofactor
Marjorie Sonnay1, Felix Zelder1
1Department of Chemistry, University of Zurich, Winterthurerstrasse 190, CH-8057 Zurich, Switzerland. felix.zelder@chem.uzh.ch.
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.
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