ArticlePloS one2013
A set of engineered Escherichia coli expression strains for selective isotope and reactivity labeling of amino acid side chains and flavin cofactors.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 22 citations in OpenAlex.
- Sequential structural changes in the monomeric LOV histidine kinase EL346 revealed by transient infrared spectroscopy.Physical chemistry chemical physics : PCCP · 2026Article
- Optimized histidine-specific isotopic labeling in proteins overproduced in Escherichia coli.Protein science : a publication of the Protein Society · 2026Article
- Signal propagation in LOV-based multidomain proteins: time-resolved infrared spectroscopy reveals the complete photocycle of YF1 and PAL.Physical chemistry chemical physics : PCCP · 2026Article
- Linear free energy relationship between reduction potential and photoreduction rate: studies on Drosophila cryptochrome.The FEBS journal · 2025Article
- How Aqueous Solvation Impacts the Frequencies and Intensities of Infrared Absorption Bands in Flavin: The Quest for a Suitable Solvent Model.Molecules (Basel, Switzerland) · 2024Article
- Spectroscopic and Computational Observation of Glutamine Tautomerization in the Blue Light Sensing Using Flavin Domain Photoreaction.Journal of the American Chemical Society · 2023Article
- Physical methods for studying flavoprotein photoreceptors.Methods in enzymology · 2019Article
- Evidence for Tautomerisation of Glutamine in BLUF Blue Light Receptors by Vibrational Spectroscopy and Computational Chemistry.Scientific reports · 2016Article
- Synthesis and application of isotopically labeled flavin nucleotides.Journal of labelled compounds & radiopharmaceuticals · 2015Article
- A proposal for a dipole-generated BLUF domain mechanism.Frontiers in molecular biosciences · 2015Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Biological reactions are facilitated by delicate molecular interactions between proteins, cofactors and substrates. To study and understand their dynamic interactions researchers have to take great care not to influence or distort the object of study. As a non-invasive alternative to a site-directed mutagenesis approach, selective isotope labeling in combination with vibrational spectroscopy may be employed to directly identify structural transitions in wild type proteins. Here we present a set of customized Escherichia coli expression strains, suitable for replacing both the flavin cofactor and/or selective amino acids with isotope enriched or chemically modified substrates. For flavin labeling we report optimized auxotrophic strains with significantly enhanced flavin uptake properties. Labeled protein biosynthesis using these strains was achieved in optimized cultivation procedures using high cell density fermentation. Finally, we demonstrate how this approach is used for a clear assignment of vibrational spectroscopic difference signals of apoprotein and cofactor of a flavin containing photoreceptor of the BLUF (Blue Light receptors Using FAD) family.
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