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Synthesis of 13C-labeled γ-hydroxybutyrates for EPR studies with 4-hydroxybutyryl-CoA dehydratase

Lookup NU author(s): Antonius Pierik, Emeritus Professor Bernard Golding


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4-Hydroxybutyryl-CoA dehydratase from Clostridium aminobutyricum catalyses the reversible dehydration of its substrate 4-hydroxybutyryl-CoA (4-HB-CoA) to crotonyl CoA. The enzyme contains one [4Fe-4S]2+ cluster and one flavin adenine dinucleotide (FAD) molecule per homotetramer. Incubation of the enzyme with its substrate under equilibrium conditions followed by freezing at 77 K induced the EPR-spectrum of a neutral flavin semiquinone (g = 2.005, linewidth 2.1 mT), while at 10 K additional signals were detected. In an attempt to characterize these signals, 4-HB-CoA molecules specifically labeled with 13C have been synthesized. This was achieved via 13C- labeled γ-butyrolactones, which were obtained from 13C-labeled bromoacetic acids by efficient synthetic routes. Incubation of the 13C-labeled 4-hydroxybutyrate-CoA molecules with 4-hydroxybutyryl-CoA dehydratase did not lead to marked broadening of the signals. © 2004 Elsevier Inc. All rights reserved.

Publication metadata

Author(s): Naser U, Pierik AJ, Scott R, Cinkaya I, Buckel W, Golding BT

Publication type: Article

Publication status: Published

Journal: Bioorganic Chemistry

Year: 2005

Volume: 33

Issue: 1

Pages: 53-66

Print publication date: 01/02/2005

ISSN (print): 0045-2068

ISSN (electronic): 1090-2120

Publisher: Elsevier


DOI: 10.1016/j.bioorg.2004.09.001

PubMed id: 15668183


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