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

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

Research output: Contribution to journal › Article › peer-review

55 Scopus citations

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 language	English (US)
Pages (from-to)	625-627
Number of pages	3
Journal	Angewandte Chemie - International Edition
Volume	37
Issue number	5
DOIs	https://doi.org/10.1002/(SICI)1521-3773(19980316)37:5<625::AID-ANIE625>3.0.CO;2-4
State	Published - Mar 16 1998
Externally published	Yes

Keywords

Bioorganic chemistry
Coenzymes
EPR spectroscopy
Isotopic labeling
Vitamin B

ASJC Scopus subject areas

Catalysis
General Chemistry

Access to Document

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

Cite this

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

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.",

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year = "1998",

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AU - Abend, Andreas

AU - Nitsche, Rainer

AU - Bandarian, Vahe

AU - Stupperich, Erhard

AU - Rétey, János

PY - 1998/3/16

Y1 - 1998/3/16

N2 - 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.

AB - 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.

KW - Bioorganic chemistry

KW - Coenzymes

KW - EPR spectroscopy

KW - Isotopic labeling

KW - Vitamin B

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