Dioldehydratase binds coenzyme B12 in the 'base-on' mode: ESR investigations on Cob(II)alamin

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

Research output: Contribution to journalArticle

51 Citations (Scopus)

Abstract

Even in the enzyme-bound state the dimethyl-benzimidazole 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 15N labeled.

Original languageEnglish (US)
Pages (from-to)625-627
Number of pages3
JournalAngewandte Chemie - International Edition
Volume37
Issue number5
DOIs
StatePublished - Mar 16 1998
Externally publishedYes

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Coenzymes
Paramagnetic resonance
Enzymes
Ligands
Salmonella
Cobalt
Nitrogen
Ions
Atoms
cobamamide
cob(II)alamin
benzimidazole

Keywords

  • Bioorganic chemistry
  • Coenzymes
  • EPR spectroscopy
  • Isotopic labeling
  • Vitamin B

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

Dioldehydratase binds coenzyme B12 in the 'base-on' mode : ESR investigations on Cob(II)alamin. / Abend, Andreas; Nitsche, Rainer; Bandarian, Vahe; Stupperich, Erhard; Rétey, János.

In: Angewandte Chemie - International Edition, Vol. 37, No. 5, 16.03.1998, p. 625-627.

Research output: Contribution to journalArticle

Abend, Andreas ; Nitsche, Rainer ; Bandarian, Vahe ; Stupperich, Erhard ; Rétey, János. / Dioldehydratase binds coenzyme B12 in the 'base-on' mode : ESR investigations on Cob(II)alamin. In: Angewandte Chemie - International Edition. 1998 ; Vol. 37, No. 5. pp. 625-627.
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