A. K. R. Junker et al 1 Investigating subtle 4f vs. 5f...
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1 Electronic Supplementary Material (ESI) for Dalton Transactions. This journal is The Royal Society of Chemistry 2018 A. K. R. Junker et al 1 Investigating subtle 4f vs. 5f... Electronic Supplementary Information for Investigating subtle 4f vs. 5f coordination differences using kinetically inert Eu(III), Tb(III), and Cm(III) complexes of a coumarin-appended 1,4,7,10- Tetraazacyclododecane-1,4,7-triacetate (DO3A) ligand Anne Kathrine R. Junker, a Gauthier J.-P. Deblonde, b Rebecca J. Abergel b * and Thomas Just Sørensen a * a. Nano-Science Center & Department of Chemistry, University of Copenhagen, Universitetsparken 5, 2100 København Ø, Denmark b. Chemical Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720, USA. Table of Content Electronic Supplementary Information for... 1 NMR and HRMS spectra of Preligand (1)... 2 NMR and HRMS spectra of Ligand (L)... 5 High-Resolution mass spectra of complexes... 8 Spectroscopy Eu.L absorption, excitation and luminescence spectra Tb.L absorption, excitation and luminescence spectra Cm.L absorption, excitation and luminescence spectra Lifetimes Quantum yield data Spectrofluorimetric Competition Batch Titrations with EDTA or DTPA Spectrofluorimetric Competition Batch Titrations with 3,4,3-LI-(HOPO) Fits from Spectrofluorimetric Competition Batch Titrations with 3,4,3-LI-(HOPO)... 34
2 A. K. R. Junker et al 2 Investigating subtle 4f vs. 5f... NMR and HRMS spectra of Preligand (1) Figure S1. 1 H-NMR spectrum of 1 (500 MHz CDCl 3). Signal at 1.21 and 3.48 ppm are residual diethylether.
3 A. K. R. Junker et al 3 Investigating subtle 4f vs. 5f... Figure S2. 13 C-NMR spectrum of 1 (126 MHz CDCl 3).
4 A. K. R. Junker et al 4 Investigating subtle 4f vs. 5f... Figure S3. HRMS spectra of 1.
5 A. K. R. Junker et al 5 Investigating subtle 4f vs. 5f... NMR and HRMS spectra of Ligand (L) Figure S4. 1 H-NMR spectrum of L (500 MHz D 2O). Signal at 1.12 ppm residual diethylether.
6 A. K. R. Junker et al 6 Investigating subtle 4f vs. 5f... Figure S5. 13 C NMR spectrum of L (126 MHz D 2O). 4 quaternary carbon signals from the coumarin are missing.
7 A. K. R. Junker et al 7 Investigating subtle 4f vs. 5f... Figure S6. HRMS spectrum of L.
8 A. K. R. Junker et al 8 Investigating subtle 4f vs. 5f... High-Resolution mass spectra of complexes Figure S7. HRMS spectrum of Eu.L.
9 A. K. R. Junker et al 9 Investigating subtle 4f vs. 5f... Figure S8. HRMS spectrum of Tb.L.
10 A. K. R. Junker et al 10 Investigating subtle 4f vs. 5f... Spectroscopy UV/VIS spectroscopy: All spectra were recorded on a Varian Cary 6000i double beam absorption spectrophotometer, using quartz cells of 1 cm path length for Eu.L and 0.01 cm for Tb.L, Cm.L. All absorbance values were corrected from the absorbance of the corresponding buffer. Luminescence spectroscopy: All steady state, excitation and emission spectra were recorded on a HORIBA Jobin Yvon IBH FluoroLog-3 spectrofluorimeter. A sub-microsecond Xenon flashlamp (Jobin Yvon, 5000XeF) was used as the light source, with an input pulse energy (100 nf discharge capacitance) of ca. 50 mj, yielding an optical pulse duration of less than 300 ns at full width at half maximum (FWHM). Spectral selection was achieved by passage through a double grating excitation monochromator (2.1 nm/mm dispersion, 1200 grooves/mm). Emission was monitored perpendicular to the excitation pulse; again with spectral selection. The time-gated emission spectrum of Tb.L was recorded on a Cary Eclipse fluorescence spectrometer with a photomultiplier tube from Agilent Technologies. For all luminescence measurements, the absorbance at the excitation wavelength and longer wavelengths was kept below 0.1 to avoid inner filter effects and intermolecular interactions. All luminescence experiments were performed in either 1 cm or 0.01 cm quartz cells. Luminescence lifetimes were determined on a HORIBA Jobin Yvon IBH FluoroLog-3 spectrofluorimeter, adapted for time-correlated single photon counting (TCSPC) and multichannel scaling (MCS) measurements. The luminescence decays were analyzed and fitted to exponential decay functions using the Origin software package.
11 A. K. R. Junker et al 11 Investigating subtle 4f vs. 5f... Eu.L absorption, excitation and luminescence spectra 1,0x10 4 8,0x10 3 ε (M -1 cm -1 ) 6,0x10 3 4,0x10 3 Eu.L 2,0x10 3 0, Figure S9. Absorption spectrum of Eu.L, 15 μm in HEPES buffer at ph Emission 407 Emission Figure S10. Excitation spectra of Eu.L, 15 μm in HEPES buffer at ph 7.4. Emission followed at 407 (black curve) and 616 nm (red curve), slits 3 nm (excitation) and 5 (emission).
12 A. K. R. Junker et al 12 Investigating subtle 4f vs. 5f Intensity (a.u) Eu.L Figure S11. Emission spectrum of Eu.L, 15 μm in HEPES buffer at ph 7.4. Excitation at 325 nm, slits 5 nm (excitation) and 3 nm (emission) Eu.L Figure S12. Zoom of emission spectrum Eu.L, focused on the Eu emission. Excitation at 325 nm, slits 5 nm (excitation) and 3 nm (emission).
13 A. K. R. Junker et al 13 Investigating subtle 4f vs. 5f... Tb.L absorption, excitation and luminescence spectra 1,0x10 4 8,0x10 3 ε (M -1 cm -1 ) 6,0x10 3 4,0x10 3 Tb.L 2,0x10 3 0, Figure S13. Absorption spectrum of Tb.L, 15 μm in HEPES buffer at ph ,0x10 8 8,0x10 7 6,0x10 7 4,0x10 7 Emission 407 Emission 545 2,0x10 7 0, Figure S14. Excitation spectra of Tb.L, 15 μm in HEPES buffer at ph 7.4. Emission followed at 407 (black curve) and 545 nm (green curve), slits 3 nm (excitation) and5 nm (emission).
14 A. K. R. Junker et al 14 Investigating subtle 4f vs. 5f Tb.L Figure S15. Emission spectrum of Tb.L, 15 μm in HEPES buffer at ph 7.4. Excitation at 325 nm, slits 5 nm (excitation) and 3 nm (emission) Tb.L Figure S16. Time gated emission spectrum of Tb.L, 15 μm in HEPES buffer at ph 7.4. Excitation at 325 nm, slits 20 nm (excitation) and 20 nm (emission), total decay time 0.01 s. delay 0.2 ms, gate time 3 ms.
15 A. K. R. Junker et al 15 Investigating subtle 4f vs. 5f... Cm.L absorption, excitation and luminescence spectra 8,0x10 4 6,0x10 4 ε (M -1 cm -1 ) 4,0x10 4 Cm.L 2,0x10 4 0, Figure S17. Absorption spectrum of Cm.L, 1.68 μm in HEPES buffer at ph Emission 609 Emission Figure S18. Excitation spectra of Cm.L, 1.68 μm in HEPES buffer at ph 7.4. Emission followed at 400 (black curve) and 609 nm (red curve), slits 3 nm (emission) and 5 nm (emission).
16 A. K. R. Junker et al 16 Investigating subtle 4f vs. 5f Intensity (a.u) Cm.L Figure S19. Emission spectra Cm.L, 1.68 μm in HEPES buffer at ph 7.4. Excitation at 325 nm, slits 5 nm (excitation) and 3 nm (emission) Cm.L Figure S20. Zoom of emission spectrum Cm.L, focused on the Cm emission. Excitation at 325 nm, slits 5 nm (excitation) and 3 nm (emission).
17 A. K. R. Junker et al 17 Investigating subtle 4f vs. 5f... Lifetimes Reduced C 491,24608 Adj. R-Squ 0,99838 Value Standard Er?$OP:F=1 y0 53,0119 0,77139?$OP:F=1 A1 2970,2511 3,68661?$OP:F=1 t1 408, ,75859?$OP:F=1 k 0, ,54149E-?$OP:F=1 tau 283, ,52581 Eu.L H 2 O ExpDec1 Fit Time ( s) Figure S21. Time-resolved emission decay profile and fit for Eu.L, 15 μm (ph 7.4 in HEPES buffer), monitored at 616 nm following 325 nm light excitation Reduced C 377,66591 Adj. R-Squ 0,99726 Value Standard Er?$OP:F=1 y0 40, ,50276?$OP:F=1 A1 1685,9076 1,26732?$OP:F=1 t1 1634,5283 2,5046?$OP:F=1 k 6,11797E- 9,3746E-7?$OP:F=1 tau 1132,9687 1,73605 Eu.L D 2 O ExpDec1 Fit Time ( s) Figure S22. Time-resolved emission decay profile and fit for Eu.L, 15 μm (ph 7.4 in D 2O HEPES buffer), monitored at 616 nm following 325 nm light excitation.
18 A. K. R. Junker et al 18 Investigating subtle 4f vs. 5f... Intensity (a.u) Reduced Chi-S Adj. R-Square Value Standard Error?$OP:F=1 y ?$OP:F=1 A ?$OP:F=1 t ?$OP:F=1 k E E-8?$OP:F=1 tau Reduced C Adj. R-Squ Value Standard E?$OP:F=1 y ?$OP:F=1 A ?$OP:F=1 t ?$OP:F=1 k E E-?$OP:F=1 tau Tb.L H 2 O ExpDec1 Fit D ExpDec1 Fit of Sheet1 D Time (ns) Figure S23. Time-resolved emission decay profile and fit for Tb.L, 15 μm(ph 7.4 in HEPES buffer), monitored at 545 nm following 325 nm light excitation. First determination (black), second determination (gray) Reduced C 3,90591E6 Adj. R-Squ 0,15816 Value Tb.L D 2 O ExpDec1 Fit Standard Er?$OP:F=1 y0 2, ,39576?$OP:F=1 A1 21, ,5449?$OP:F=1 t1 1,23508E6 973,15252?$OP:F=1 k 8,09667E- 4,16774E-?$OP:F=1 tau ,41 674, Time (ns) Figure S24. Time-resolved emission decay profile and fit for Tb.L, 15 μm (ph 7.4 in D 2O HEPES buffer), monitored at 545 nm following 325 nm light excitation.
19 A. K. R. Junker et al 19 Investigating subtle 4f vs. 5f... Intensity (a.u) Reduced C 349,57267 Adj. R-Squ 0,99312 Value Standard Er?$OP:F=1 y0 64,6181 0,65498?$OP:F=1 A1 1318,3677 3,72721?$OP:F=1 t1 403, ,55529?$OP:F=1 k 0, ,56941E-?$OP:F=1 tau 279, ,07805 Cm.L H 2 0 ExpDec1 Fit Time (ns) Figure S25. Time-resolved emission decay profile and fit for Cm.L, 1.68 μm (ph 7.4 in HEPES buffer), monitored at 610 nm following 325 nm light excitation Time (us) Residual S Pearson's r Adj. R-Squ Value Standard E Intercept Slope Cm.L Linear fit % D2O Figure S26. Emission decay profile observed for Cm.L with increasing volumic ratio of D 2O. The data was fitted to a linear decay to determine the associated lifetime.
20 A. K. R. Junker et al 20 Investigating subtle 4f vs. 5f... Quantum yield data 1.5x x10 9 Integrated Emission 1.0x x10 7 Residual S E1 Pearson's r Adj. R-Squ Value Standard E Slope E E7 Residual S E17 Pearson's r Adj. R-Squ Value Standard E Slope E E9 Quinine Sulfate Linear Fit 4.0x x10 9 Eu Emission Linear Fit Absorption Figure S27. Quantum yield determination for the Eu(III) centred emission from Eu.L ( nm). ph 7.4 (0.1 M HEPES Buffer). The red line is a linear fit of the data for the sample and the black line is a linear fit of the data for the reference quinine sulfate Integrated Emission Residual S Pearson's r Adj. R-Squ Value Standard E Slope Residual S E7 Pearson's r Adj. R-Squ Value Standard E Slope Quinine Sulfate Linear Fit Coumarin emission Linear Fit Absorption Figure S28. Quantum yield determination for the coumarin emission from Eu.L at ph 7.4 (0.1 M HEPES Buffer). The red line is a linear fit of the data for the sample and the black line is a linear fit of the data for the reference quinine sulfate.
21 A. K. R. Junker et al 21 Investigating subtle 4f vs. 5f Residual S Pearson's r Adj. R-Squ Value Standard E Slope Integrated Emission Residual S E E7 Pearson's r Adj. R-Squ Value Standard E Slope Quinine Sulfate Linear Fit Coumarin Emission Linear Fit Absorption Figure S29. Quantum yield determination for the coumarin emission from Tb.L at ph 7.4 (0.1 M HEPES Buffer). The red line is a linear fit of the data for the sample and the black line is a linear fit of the data for the reference quinine sulfate. 9.0x x10 9 Residual Sum of E13 Pearson's r Adj. R-Square Value Standard Err Integrated Emission 6.0x x10 7 Slope E E8 Residual Sum of E17 Pearson's r Adj. R-Square Value Standard Erro Slope E E9 Emission Cm Linear Fit 4.0x x10 9 Quinine Sulfate Linear Fit Absorption Figure S30. Quantum yield determination for Cm(III) centred emission from Cm.L. ph 7.4 (0.1 M HEPES Buffer). The red line is a linear fit of the data for the sample and the black line is a linear fit of the data for the reference quinine sulfate.
22 A. K. R. Junker et al 22 Investigating subtle 4f vs. 5f... Spectrofluorimetric Competition Batch Titrations with EDTA or DTPA Series of aqueous samples containing a fixed concentration of Eu.L (1.4 μm) and a varying amount of ligand competitor (0 to 10 equivalents of EDTA or 0 to 500 equivalents of DTPA) were prepared in KCl 0.1 M/HEPES buffer 10 mm. For the first attempt to challenge Eu.L with EDTA, the samples were equilibrated in a thermostatic shaker at 60 C (4 days), and then at 25 C (3 days) until equilibrium was reached and measurements were stable (7 days). At the concentration used in these experiments, Eu(III) luminescence from Eu.L can be easily observed whereas Eu(III) luminescence from Eu.EDTA was too weak to be observed. Hence, a complete disappearance of the Eu(III) emission was expected if the Eu(III) was complexed by EDTA at the expense of L. As shown in Figure S27, no significant change was observed in the steady state emission spectra of the samples indicating that Eu(III) remained bound to L. The second attempt used DTPA as challenging ligand since the Eu.DTPA complex is more stable that its EDTA counterpart. All samples were sealed in glass vials and equilibrated in a thermostatic shaker at 60 C (4 days), and 25 C (3 days) until equilibrium was reached and measurements were stable (7 days). The emission spectrum of each solution was measured using a 0.1 cm quartz cell. A drop in the emission intensity (about a 5-fold decrease) of the Eu(III) centered emission from Eu.L was expected in the case of a ligand exchange between and L and DTPA due to the lower brightness of the Eu.DTPA complex. As shown in Figure S28, no significant change was observed in the steady state emission spectra of the samples indicating that the Eu.L complex is too inert to be challenged by DPTA, even using 500 equivalents.
23 A. K. R. Junker et al 23 Investigating subtle 4f vs. 5f Series Eu.L vs EDTA 2,0x10 6 1,5x10 6 1,0x eq 0.5 eq 1 eq 2 eq 3 eq 4 eq 5 eq 6 eq 7 eq 8 eq 9 eq 10 eq 5,0x10 5 0, x10 6 Intensity at 615 nm (a.u) 1.6x x x x10 5 Eu Emission Equivalent EDTA Figure S31. Top: Spectrofluorimetric competition titration of Eu.L against EDTA ([Eu.L] = 1.4 μm, [EDTA] from 0 to 13 μm, KCl 10 mm, 0.1 M HEPES, ph 7.4, 25 C, exc = 325 nm) Bottom: change in emission intensity at 615 nm as a function of equivalents of competitor added.
24 A. K. R. Junker et al 24 Investigating subtle 4f vs. 5f Series Eu.L vs DTPA 5,0x10 5 4,0x10 5 3,0x10 5 2,0x eq 5 eq 10 eq 15 eq 25 eq 30 eq 35 eq 40 eq 45 eq 50 eq Eu-DTPA 1,0x10 5 0, x10 6 Intensity at 615 nm (a.u.) 8.0x x x x10 5 Eu Intensity Equivalent DTPA Figure S32. Top: Spectrofluorimetric competition titration of Eu.L against DTPA ([Eu.L] = 1.4 μm, [DTPA] from 0 to 70 μm, KCl 0.1 M, 10 mm HEPES, ph 7.4, 25 C, exc = 325 nm). Bottom: change in emission intensity at 615 nm as a dunction of equivalents of competitor added.
25 A. K. R. Junker et al 25 Investigating subtle 4f vs. 5f Series Eu.L vs DTPA 5,0x10 5 4,0x10 5 3,0x10 5 2,0x eq 100 eq 150 eq 200 eq 250 eq 300 eq 350 eq 400 eq 450 eq 500 eq 1,0x10 5 0, ,0x10 5 Intensity at 615 nm (a.u.) 4,5x10 5 4,0x10 5 Eu Intensity 3,5x Equivalent DTPA Figure S33. Top: Spectrofluorimetric competition titration of Eu.L against DTPA ([Eu.L] = 1.4 μm, [DTPA] from 0 to 700 μm, KCl 0.1 M, 10 mm HEPES, ph 7.4, 25 C, exc = 325 nm). Bottom: change in emission intensity at 615 nm as a function of equivalents of competitor added.
26 A. K. R. Junker et al 26 Investigating subtle 4f vs. 5f... Spectrofluorimetric Competition Batch Titrations with 3,4,3-LI-(HOPO) Series of aqueous samples containing a fixed concentration of M.L (1.4 μm of Eu.L or 1.2 μm of Tb.L or 0.11 μm of Cm.L) and a varying amount of ligand competitor (0 to 50 equivalents of 3,4,3-LI(1,2-HOPO) prepared in KCl 0.1 M/HEPES buffer 10 mm. All samples were equilibrated in a thermostatic shaker at 60 C (4 days), and 25 C (3 days) until equilibrium was reached and measurements were stable (7 days). The emission spectrum of each solution was measured using a 0.1 cm quartz cell. In this case, an increase in the emission intensity from Eu(III), Tb(III), or Cm(III) was expected since the complexes of 3,4,3-LI(1,2-HOPO) are brighter that the corresponding complexes with L. Changes in the emission features (i.e. slight shift of the emission bands and changes in the emission line ratio) was also expected if the M.L complexes were in equilibrium with their 3,4,3-LI(1,2-HOPO) analogues. 3,4,3-LI(1,2-HOPO) was found to be strong enough to displace Eu(III), Tb(III), and Cm(III) from their complexes with L, as displayed in the figures S31, S33, and S35. Data Treatment. All thermodynamic data sets were imported into the refinement program HypSpec and analyzed by nonlinear least-squares refinement. All equilibrium constants were defined as cumulative formation constants, β mlh according to equation (2), where the metal and ligand are designed as M and L, respectively. mm + ll + hh [M m L l H h ] ; β mlh = [M ml l H h ] [M] m [L] l [H] h (S2) All metal and ligand concentrations were held at estimated values determined from the volume of standardized stock solutions. The emission spectra of the complexes were recorded. The refinements of the overall formation constants included the literature values for the protonation constants in each case and the metal hydrolysis products, the equilibrium constants of which was fixed to the literature values. The entire procedure (sample preparation, equilibration, spectrofluorimetric measurements, and data treatment) was, at least, duplicate for each metal-ligand system.
27 A. K. R. Junker et al 27 Investigating subtle 4f vs. 5f Series Eu.L: 2,5x10 7 2,0x10 7 1,5x10 7 1,0x10 7 5,0x eq 3,4,3-HOPO 0 eq 3,4,3-HOPO 0, x10 7 Intensity at 617 nm (a.u.) 1.5x x x10 6 Eu Intensity Equivalent 3,4,3-HOPO Figure S34. Top: Spectrofluorimetric competition titration of Eu.L (1. Series) against 3,4,3-LI(HOPO) ([Eu.L] = 1.4 μm, [HOPO] from 0 to 70 μm, KCl 0.1 M, 10 mm HEPES, ph 7.4, 25 C, exc = 325 nm). Bottom: change in emission intensity at 617 nm as a function of equivalents of competitor added.
28 A. K. R. Junker et al 28 Investigating subtle 4f vs. 5f Series EuL: 2,4x10 7 2,2x10 7 2,0x10 7 1,8x10 7 1,6x10 7 1,4x10 7 1,2x10 7 1,0x10 7 8,0x10 6 6,0x10 6 4,0x10 6 2,0x eq 3,4,3-HOPO 0 eq 3,4,3-HOPO 0, x10 7 Intensity at 617 nm (a.u.) 1.5x x x10 6 Eu Intensity Equivalent 3,4,3-HOPO Figure S35. Top: Spectrofluorimetric competition titration of Eu.L (2. Series) against 3,4,3-LI(HOPO) ([Eu.L] = 1.4 μm, [HOPO] from 0 to 14 μm, KCl 0.1 M, 10 mm HEPES, ph 7.4, 25 C, exc = 325 nm). Bottom: change in emission intensity at 617 nm as a function of equivalents of competitor added.
29 A. K. R. Junker et al 29 Investigating subtle 4f vs. 5f Series Eu.L: 2,0x10 7 1,5x eq 3,4,3-HOPO 1,0x10 7 5,0x eq 3,4,3-HOPO 0, x x10 7 Intensity at 617 nm (a.u.) 1.4x x x x x x x Eu Intensity Equivalent 3,4,3-HOPO Figure S36. Top: Example of batch spectrofluorimetric competition titration of Eu.L against 3,4,3-LI(HOPO) ([Eu.L] = 1.4 μm, [HOPO] from 0 to 3μM, KCl 0.1 M, 10 mm HEPES, ph 7.4, 25 C, exc = 325 nm). Bottom: change in emission intensity at 617 nm as a function of equivalents of competitor added.
30 A. K. R. Junker et al 30 Investigating subtle 4f vs. 5f Series Tb.L: 2,5x10 6 2,0x eq 3,4,3-HOPO Intensity (a.u) 1,5x10 6 1,0x eq 3,4,3-HOPO 5,0x10 5 0, x x10 6 Intensity at 544 nm (a.u.) 1.4x x x x x10 5 Tb Emission 4.0x x Equivalent 3,4,3-HOPO Figure S37. Top: Spectrofluorimetric competition titration of Tb.L against 3,4,3-LI(HOPO) ([Tb.L] = 1.2 μm, [HOPO] from 0 to 12 μm, KCl 0.1 M, 10 mm HEPES, ph 7.4, 25 C, exc = 325 nm). Bottom: change in emission intensity at 544 nm as a function of equivalents of competitor added.
31 A. K. R. Junker et al 31 Investigating subtle 4f vs. 5f Series Tb.L: eq 3,4,3-HOPO eq 3,4,3-HOPO x10 6 Intensity at 544 nm (a.u.) 2.0x x x x10 5 Tb Emission Equivalent 3,4,3-HOPO Figure S38. Top: Example of batch spectrofluorimetric competition titration of Tb.L against 3,4,3-LI(HOPO) ([Tb.L] = 1.2 μm, [HOPO] from 0 to 1.2 μm, KCl 0.1 M, 10 mm HEPES, ph 7.4, 25 C, exc = 325 nm). Bottom: change in emission intensity at 544 nm as a function of equivalents of competitor added.
32 A. K. R. Junker et al 32 Investigating subtle 4f vs. 5f Series Cm.L: 2,2x10 7 2,0x10 7 1,8x10 7 1,6x10 7 1,4x10 7 1,2x10 7 1,0x10 7 8,0x10 6 6,0x10 6 4,0x10 6 2,0x eq 3,4,3-HOPO 0 eq 3,4,3-HOPO 0, x10 7 Intensity at 610 nm (a.u.) 1.2x x x x x x10 6 Cm Emission Equivalent 3,4,3-HOPO Figure S39. Top: Example of batch spectrofluorimetric competition titration of Cm.L (Series 1) against 3,4,3-LI(HOPO) ([Cm.L] = 0.11 μm, [HOPO] from 0 to 0.2 μm, KCl 0.1 M, 10 mm HEPES, ph 7.4, 25 C, exc = 325 nm). Bottom: change in emission intensity at 610 nm as a function of equivalents of competitor added.
33 A. K. R. Junker et al 33 Investigating subtle 4f vs. 5f Series Cm.L: 5,0x10 6 4,0x10 6 3,0x10 6 2,0x eq 3,4,3-HOPO 1,0x eq 3,4,3-HOPO 0, x10 6 Intensity at 610 nm (a.u.) 2.5x x x x x10 5 Cm emission Equivalent 3,4,3-HOPO Figure S40. Top: Spectrofluorimetric competition titration of Cm.L (Series 2) against 3,4,3-LI(HOPO) ([Cm.L] = 0.11 μm, [HOPO] from 0 to 0.2 μm, KCl 0.1 M, 10 mm HEPES, ph 7.4, 25 C, exc = 325 nm). Bottom: change in emission intensity at 610 nm as a function of equivalents of competitor added.
34 Intensity at 617 nm (a.u.) Intensity at 617 nm (a.u.) A. K. R. Junker et al 34 Investigating subtle 4f vs. 5f... Fits from Spectrofluorimetric Competition Batch Titrations with 3,4,3-LI- (HOPO) 2,0E+07 1,5E+07 1,0E+07 5,0E+06 Exp. Calc. 0,0E Equivalent of 3,4,3-LI(1,2-HOPO) Figure S41. HypSpec fit (squares) of data (crosses) from spectrofluorimetric competition titration of Eu.L (1. Series) against 3,4,3-LI(HOPO) ([Eu.L] = 1.4 μm, [HOPO] from 0 to 70 μm, KCl 0.1 M, 10 mm HEPES, ph 7.4, 25 C, exc = 325 nm). 2,0E+07 1,5E+07 1,0E+07 5,0E+06 Exp. 1,0E Equivalent of 3,4,3-LI(1,2-HOPO) Figure S42. HypSpec fit (squares) of data (crosses) from spectrofluorimetric competition titration of Eu.L (2. Series) against 3,4,3-LI(HOPO) ([Eu.L] = 1.4 μm, [HOPO] from 0 to 14 μm, KCl 0.1 M, 10 mm HEPES, ph 7.4, 25 C, exc = 325 nm).
35 Intensity at 544 nm (a.u.) Intensity at 617 nm (a.u.) A. K. R. Junker et al 35 Investigating subtle 4f vs. 5f... 2,0E+07 1,5E+07 1,0E+07 5,0E+06 0,0E ,5 1 1,5 2 2,5 Equivalent of 3,4,3-LI(1,2-HOPO) Exp. Calc. Pure EuL Figure S43. HypSpec fit (squares) of data (crosses) from spectrofluorimetric competition titration of Eu.L against 3,4,3- LI(HOPO) ([Eu.L] = 1.4 μm, [HOPO] from 0 to 3μM, KCl 0.1 M, 10 mm HEPES, ph 7.4, 25 C, exc = 325 nm). 1,6E+06 1,4E+06 1,2E+06 1,0E+06 8,0E+05 6,0E+05 4,0E+05 2,0E+05 0,0E ,2 0,4 0,6 0,8 1 Equivalent of 3,4,3-LI(1,2-HOPO) Exp. Calc. Figure S44. HypSpec fit (squares) of data (crosses) from spectrofluorimetric competition titration of Tb.L against 3,4,3- LI(HOPO) ([Tb.L] = 1.2 μm, [HOPO] from 0 to 1.2 μm, KCl 0.1 M, 10 mm HEPES, ph 7.4, 25 C, exc = 325 nm).
36 Intensity at 610 nm (a.u.) A. K. R. Junker et al 36 Investigating subtle 4f vs. 5f... 2,0E+07 1,5E+07 1,0E+07 5,0E+06 Exp. 0,0E+00 0,0 0,5 1,0 1,5 2,0 2,5 Equivalent of 3,4,3-LI(1,2-HOPO) Figure S45. HypSpec fit (squares) of data (crosses) from spectrofluorimetric competition titration of Cm.L (Series 1) against 3,4,3-LI(HOPO) ([Cm.L] = 0.11 μm, [HOPO] from 0 to 0.2 μm, KCl 0.1 M, 10 mm HEPES, ph 7.4, 25 C, exc = 325 nm).
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