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. 1998 Mar 16;37(5):625-627.
doi: 10.1002/(SICI)1521-3773(19980316)37:5<625::AID-ANIE625>3.0.CO;2-4.

Dioldehydratase Binds Coenzyme B12 in the "Base-On" Mode: ESR Investigations on Cob(II)alamin

Andreas Abend  1 , Rainer Nitsche  2 , Vahe Bandarian  1 , Erhard Stupperich  3 , János Rétey  2
Affiliations

Dioldehydratase Binds Coenzyme B12 in the "Base-On" Mode: ESR Investigations on Cob(II)alamin

Andreas Abend et al. Angew Chem Int Ed Engl. .

Abstract

Even in the enzyme-bound state the dimethylbenzimidazole ligand in the dioldehydratase from Salmonella typhimurium remains bound to the cobalt ion in contrast to some coenzyme B12 -dependent enzymes. Direct, ESR spectroscopic proof for this "base-on" binding mode was obtained by using a coenzyme in which one of the nitrogen atoms of the dimethylbenzimidazole ligand was 15 N labeled (see schematic representation on the right).

Keywords: Bioorganic chemistry; Coenzymes; EPR spectroscopy; Isotopic labeling; Vitamin B12.

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