ArticleJournal of molecular biology2013
(77)Se enrichment of proteins expands the biological NMR toolbox.
Article in Journal of molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
14 citing papers in PubMed, 38 citations in OpenAlex.
- Review
- Exploring Sulfur Sites in Proteins via Triple-ResonanceJournal of the American Chemical Society · 2023Article
- Dissolution Dynamic Nuclear Polarization of theAnalysis & sensing · 2023Article
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- Selenium Valence-to-Core X-ray Emission Spectroscopy and Kβ HERFD X-ray Absorption Spectroscopy as Complementary Probes of Chemical and Electronic Structure.Inorganic chemistry · 2022Article
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- Assessing the dispersive and electrostatic components of the selenium-aromatic interaction energy by DFT.Journal of molecular modeling · 2017Article
- Utilizing Selenocysteine for Expressed Protein Ligation and Bioconjugations.Journal of the American Chemical Society · 2017Article
- Probing pattern and dynamics of disulfide bridges using synthesis and NMR of an ion channel blocker peptide toxin with multiple diselenide bonds.Chemical science · 2016Article
- (77)Se chemical shift tensor of L-selenocystine: experimental NMR measurements and quantum chemical investigations of structural effects.The journal of physical chemistry. B · 2015Article
- Redox active motifs in selenoproteins.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Site-specific insertion of selenium into the redox-active disulfide of the flavoprotein augmenter of liver regeneration.Archives of biochemistry and biophysics · 2014Article
- Article
- Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Sulfur, a key contributor to biological reactivity, is not amendable to investigations by biological NMR spectroscopy. To utilize selenium as a surrogate, we have developed a generally applicable (77)Se isotopic enrichment method for heterologous proteins expressed in Escherichia coli. We demonstrate (77)Se NMR spectroscopy of multiple selenocysteine and selenomethionine residues in the sulfhydryl oxidase augmenter of liver regeneration (ALR). The resonances of the active-site residues were assigned by comparing the NMR spectra of ALR bound to oxidized and reduced flavin adenine dinucleotide. An additional resonance appears only in the presence of the reducing agent and disappears readily upon exposure to air and subsequent reoxidation of the flavin. Hence, (77)Se NMR spectroscopy can be used to report the local electronic environment of reactive and structural sulfur sites, as well as changes taking place in those locations during catalysis.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.