ArticleProceedings of the National Academy of Sciences of the United States of America1997
Choline monooxygenase, an unusual iron-sulfur enzyme catalyzing the first step of glycine betaine synthesis in plants: prosthetic group characterization and cDNA cloning.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.
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Who cites it
64 citing papers in PubMed, 256 citations in OpenAlex.
- Transcriptional reprogramming under drought reveals divergent adaptive strategies in Quinoa.BMC plant biology · 2025Article
- Overexpression ofBiomolecules · 2025Article
- Advances in the Biosynthetic Regulation and Functional Mechanisms of Glycine Betaine for Enhancing Plant Stress Resilience.International journal of molecular sciences · 2025Review
- Bacterial osmoprotectants-a way to survive in saline conditions and potential crop allies.FEMS microbiology reviews · 2025Review
- Drought Stress Tolerance in Vegetables: The Functional Role of Structural Features, Key Gene Pathways, and Exogenous Hormones.International journal of molecular sciences · 2023Review
- Monitoring Drought Tolerance in Oil Palm: Choline Monooxygenase as a Novel Molecular Marker.Plants (Basel, Switzerland) · 2023Article
- Salt and drought stress-mitigating approaches in sugar beet (Beta vulgaris L.) to improve its performance and yield.Planta · 2023Review
- Contrasting Mechanisms of Aromatic and Aryl-Methyl Substituent Hydroxylation by the Rieske Monooxygenase Salicylate 5-Hydroxylase.Biochemistry · 2023Article
- Exploring the medicinally important secondary metabolites landscape through the lens of transcriptome data in fenugreek (Trigonella foenum graecum L.).Scientific reports · 2022Article
- Exploring Thermal Sensitivities and Adaptations of Oxidative Phosphorylation Pathways.Metabolites · 2022Review
- Alteration of proteome in germinating seedlings of piegonpea (Physiology and molecular biology of plants : an international journal of functional plant biology · 2021Article
- Article
- Metabolic engineering of osmoprotectants to elucidate the mechanism(s) of salt stress tolerance in crop plants.Planta · 2021Review
- Heterologous Production of Glycine Betaine UsingFrontiers in bioengineering and biotechnology · 2021Article
- Unleashing the Synthetic Power of Plant Oxygenases: From Mechanism to Application.Plant physiology · 2019Review
- Functional Characterization and Evolutionary Analysis of Glycine-Betaine Biosynthesis Pathway in Red SeaweedMarine drugs · 2019Article
- Spatial and Temporal Profile of Glycine Betaine Accumulation in Plants Under Abiotic Stresses.Frontiers in plant science · 2019Review
- A Protochlorophyllide (Pchlide)Frontiers in plant science · 2019Article
- Roles and maturation of iron-sulfur proteins in plastids.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Review
- Identification ofPlant direct · 2018Article
4 more citing papers are in PubMed but not listed here.
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Authors and funding
9 authors at 5 institutions in 2 countries.
Funding
Abstract
Plants synthesize the osmoprotectant glycine betaine via the route choline --> betaine aldehyde --> glycine betaine. In spinach, the first step is catalyzed by choline monooxygenase (CMO), a ferredoxin-dependent stromal enzyme that has been hypothesized to be an oligomer of identical subunits and to be an Fe-S protein. Analysis by HPLC and matrix-assisted laser desorption ionization MS confirmed that native CMO contains only one type of subunit (Mr 42,864). Determination of acid-labile sulfur and nonheme iron demonstrated that there is one [2Fe-2S] cluster per subunit, and EPR spectral data indicated that this cluster is of the Rieske type--i.e., coordinated by two Cys and two His ligands. A full-length CMO cDNA (1,622 bp) was cloned from spinach using a probe generated by PCR amplification for which the primers were based on internal peptide sequences. The ORF encoded a 440-amino acid polypeptide that included a 60-residue transit peptide. The deduced amino acid sequence included two Cys-His pairs spaced 16 residues apart, a motif characteristic of Rieske-type Fe-S proteins. Larger regions that included this motif also showed some sequence similarity (approximately 40%) to Rieske-type proteins, particularly bacterial oxygenases. Otherwise there was very little similarity between CMO and proteins from plants or other organisms. RNA and immunoblot analyses showed that the expression of CMO in leaves increased several-fold during salinization. We conclude that CMO is a stress-inducible representative of a new class of plant oxygenases.
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