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Dioldehydratase Binds Coenzyme B 12 in the “Base‐On” Mode: ESR Investigations on Cob( II )alamin
Author(s) -
Abend Andreas,
Nitsche Rainer,
Bandarian Vahe,
Stupperich Erhard,
Rétey János
Publication year - 1998
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/(sici)1521-3773(19980316)37:5<625::aid-anie625>3.0.co;2-4
Subject(s) - chemistry , base (topology) , cofactor , stereochemistry , biochemistry , mathematics , enzyme , mathematical analysis
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 B 12 ‐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).