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

作者信息

Abend Andreas, Nitsche Rainer, Bandarian Vahe, Stupperich Erhard, Rétey János

机构信息

Institute for Enzyme Research, University of Wisconsin-Madison 1710 University Avenue, Madison, WI 53705-4098 (USA).

Institut für Organische Chemie der Universität, Richard-Willstätter-Allee, D-76128 Karlsruhe (Germany), Fax: (+49) 721-6084823.

出版信息

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

DOI:10.1002/(SICI)1521-3773(19980316)37:5<625::AID-ANIE625>3.0.CO;2-4

PMID:29711083

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 B -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 N labeled (see schematic representation on the right).

摘要