Abstract
The flavin-dependent enzyme 2-haloacrylate hydratase (2-HAH) catalyzes the conversion of 2-chloroacrylate, a major component in the manufacture of acrylic polymers, to pyruvate. The enzyme was expressed in Escherichia coli, purified, and characterized. 2-HAH was shown to be monomeric in solution and contained a non-covalent, yet tightly bound, flavin adenine dinucleotide (FAD). Although the catalyzed reaction was redox-neutral, 2-HAH was active only in the reduced state. A covalent flavin-substrate intermediate, consistent with the flavin-acrylate iminium ion, was trapped with cyanoborohydride and characterized by mass spectrometry. Small-angle X-ray scattering was consistent with 2-HAH belonging to the succinate dehydrogenase/fumarate reductase family of flavoproteins. These studies establish 2-HAH as a novel noncanonical flavoenzyme.
Recommended Citation
Y. Dai et al., "Flavin-N5 Covalent Intermediate in a Nonredox Dehalogenation Reaction Catalyzed by an Atypical Flavoenzyme," ChemBioChem, vol. 19, no. 1, pp. 53 - 57, Wiley; Wiley-VCH Verlag, Jan 2018.
The definitive version is available at https://doi.org/10.1002/cbic.201700594
Department(s)
Chemistry
Publication Status
Full Access
Keywords and Phrases
covalent adduct; dehalogenation; flavin; iminium adduct; non-redox reactions
International Standard Serial Number (ISSN)
1439-7633; 1439-4227
Document Type
Article - Journal
Document Version
Citation
File Type
text
Language(s)
English
Rights
© 2024 Wiley; Wiley-VCH Verlag, All rights reserved.
Publication Date
04 Jan 2018
PubMed ID
29116682
Comments
National Science Foundation, Grant CHE-1506206