Abstract
Cupriavidus taiwanensis is a nitrogen-fixing bacterium found in root nodules of the invasive tropical weed Mimosa pudica . C. taiwanensis has been shown to grow in environments contaminated with heavy metals such as Pb, Cu, and Cd. Taiwachelin, a recently identified siderophore produced by C. taiwanensis , is an iron chelator that contains a hydroxamate functional group for metal binding. In its biosynthesis, a flavin-dependent N-monooxygenase (NMO) was predicted to hydroxylate l -ornithine, leading to formation of the metal binding hydroxamate moiety. Here, we report the cloning, expression, and biochemical characterization of this enzyme, herein referred to as CtNMO. CtNMO was isolated with bound FAD and catalyzed the hydroxylation of l -ornithine with a k cat of 0.72 ± 0.04 s−1 and a K M of 156 ± 26 μM. A ∼25-fold preference for NADPH over NADH was observed. Expression of CtNMO as a fusion to maltose-binding protein resulted in enhanced enzymatic activity. These results validate CtNMO as an efficient l -ornithine hydroxylase and establish its potential utility in future applications, including bioremediation.
Recommended Citation
A. J. Gringer et al., "Hydroxamate Formation in the Lipopeptide Containing Siderophore Taiwachelin," Biochemistry and Biophysics Reports, vol. 46, article no. 102660, Elsevier B. V., Jun 2026.
The definitive version is available at https://doi.org/10.1016/j.bbrep.2026.102660
Department(s)
Chemistry
Publication Status
Open Access
International Standard Serial Number (ISSN)
2405-5808
Document Type
Article - Journal
Document Version
Citation
File Type
text
Language(s)
English
Rights
© 2026 Elsevier B. V., All rights reserved.
Creative Commons Licensing
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 4.0 License.
Publication Date
01 Jun 2026
Comments
Virginia Polytechnic Institute and State University, Grant None