Academic Journal
Binding Affinity Determines the Success of Endogenous CuII-NTA Spin Labeling for In-Cell Electron Paramagnetic Resonance Distance Measurements.
| Title: | Binding Affinity Determines the Success of Endogenous CuII-NTA Spin Labeling for In-Cell Electron Paramagnetic Resonance Distance Measurements. |
|---|---|
| Authors: | Limbach Y; EaStCHEM School of Chemistry, Biomedical Sciences Research Complex and Centre of Magnetic Resonance, University of St. Andrews, North Haugh, St Andrews, KY16 9ST Scotland, U.K.; Clausius-Institute for Physical and Theoretical Chemistry, University of Bonn, Wegelerstr. 12, 53115 Bonn, Germany., Ackermann K; EaStCHEM School of Chemistry, Biomedical Sciences Research Complex and Centre of Magnetic Resonance, University of St. Andrews, North Haugh, St Andrews, KY16 9ST Scotland, U.K., Schiemann O; Clausius-Institute for Physical and Theoretical Chemistry, University of Bonn, Wegelerstr. 12, 53115 Bonn, Germany., Bode BE; EaStCHEM School of Chemistry, Biomedical Sciences Research Complex and Centre of Magnetic Resonance, University of St. Andrews, North Haugh, St Andrews, KY16 9ST Scotland, U.K. |
| Source: | The journal of physical chemistry letters [J Phys Chem Lett] 2026 Jun 18; Vol. 17 (24), pp. 6736-6744. Date of Electronic Publication: 2026 Jun 05. |
| Publication Type: | Journal Article |
| Language: | English |
| Journal Info: | Publisher: American Chemical Society Country of Publication: United States NLM ID: 101526034 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1948-7185 (Electronic) Linking ISSN: 19487185 NLM ISO Abbreviation: J Phys Chem Lett Subsets: MEDLINE |
| Imprint Name(s): | Original Publication: Washington, D.C. : American Chemical Society |
| MeSH Terms: | Copper*/chemistry , Nitrilotriacetic Acid*/chemistry , Spin Labels*, Electron Spin Resonance Spectroscopy/methods ; Escherichia coli/chemistry ; Escherichia coli/metabolism ; Histidine/chemistry ; Binding Sites |
| Abstract: | In-cell electron paramagnetic resonance (EPR) spectroscopy requires robust spin-labeling strategies compatible with cellular conditions. CuII-NTA coordination to genetically engineered double-histidine (dHis) motifs has shown promise for endogenous labeling in Escherichia coli. Here, we evaluated the effect of varying CuII-NTA affinity on the success of these experiments. Relaxation induced dipolar modulation enhancement (RIDME)-based titrations revealed dissociation constants (K |
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| Substance Nomenclature: | 789U1901C5 (Copper) 0 (Spin Labels) 4QD397987E (Histidine) KA90006V9D (Nitrilotriacetic Acid) |
| Entry Date(s): | Date Created: 20260605 Date Completed: 20260618 Latest Revision: 20260813 |
| Update Code: | 20260813 |
| PubMed Central ID: | PMC13288622 |
| DOI: | 10.1021/acs.jpclett.6c01384 |
| PMID: | 42246266 |
| Database: | MEDLINE |
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