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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.
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
URL: http://dx.doi.org/10.1016/j.bioorg.2004.09.001
DOI: 10.1016/j.bioorg.2004.09.001
PubMed id: 15668183
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