Solutions of the irritant (1 M) and N-acetyl-l -cysteine methyl ester (1 M) in CDCl3 were prepared. The irritant solution (300 μl) was added to the thiol solution (300 μl) in a 5 mm NMR tube. Kinetic measurements were recorded at 14.1 T using the Bruker AVIII 600. The temperature was regulated using a standard broker BVT system. Spectra were recorded at 25°C after mixing (time from start t=0 min) and later (t=2 h). The temperature was raised to 37°C and spectra recorded 2 and 4 h later (t=4 h and 6 h). The temperature was returned to 25°C and spectra recorded after 4 h (t=10 h) and 14 h (t=24 h). The percentage of product was calculated at each interval by integrating the relevant signals.
Aviii 600
Manufactured by Bruker
Sourced in Germany
The AVIII 600 is a high-performance nuclear magnetic resonance (NMR) spectrometer produced by Bruker. It operates at a proton frequency of 600 MHz and is designed for advanced NMR analysis and research applications.
Automatically generated - may contain errors
Lab products found in correlation
Drx 500, by Bruker (3 mentions)
Aviii 900, by Bruker (3 mentions)
Aviii 800, by Bruker (3 mentions)
Lsm 880 microscope, by Zeiss (2 mentions)
390 lc mds system, by Agilent Technologies (2 mentions)
Rt mt autosampler, by Agilent Technologies (2 mentions)
Dpx 300, by Bruker (2 mentions)
Av neo 500, by Bruker (2 mentions)
Aviii 500, by Bruker (2 mentions)
Av 400, by Bruker (2 mentions)
Vector 22 ftir spectrometer, by Bruker (1 mentions)
1200 series system, by Agilent Technologies (1 mentions)
Amazon sl ion trap mass spectrometer, by Bruker (1 mentions)
2400 chn elemental analyzer, by PerkinElmer (1 mentions)
Xbridge c18 column, by Agilent Technologies (1 mentions)
Maxis uhr esi time of flight mass spectrometer, by Bruker (1 mentions)
Avance 3 500, by Bruker (1 mentions)
Milli q advantage, by Merck Group (1 mentions)
Lambda 35 uv vis spectrophotometer, by PerkinElmer (1 mentions)
Aviii 600 spectrometer, by Bruker (1 mentions)
28 protocols using aviii 600
1
Kinetic Study of Thiol-Irritant Reaction
2
Characterization of Polymeric Materials
3
Synthesis and Characterization of K2[PtCl4]
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Potassium tetrachloridoplatinate (K2[PtCl4]) was purchased from Johnson Matthey (Switzerland). Water for synthesis was taken from a reverse osmosis system. For HPLC measurements Milli-Q water (18.2 MΩ cm, Merck Milli-Q Advantage, Darmstadt, Germany) was used. Other chemicals and solvents were purchased from commercial suppliers (Sigma Aldrich, Merck and Fisher Scientific). Electrospray ionization (ESI) mass spectra were recorded on a Bruker Amazon SL ion trap mass spectrometer in positive and/or negative mode by direct infusion. High resolution mass spectra were measured on a Bruker maXis™ UHR ESI time of flight mass spectrometer. One- and two-dimensional 1H-NMR and 13C-NMR spectra were recorded on a Bruker Avance III 500 or AV III 600 spectrometer at 298 K. For 1H-NMR spectra the solvent residual peak was taken as internal reference. Elemental analysis measurements were performed on a PerkinElmer 2400 CHN Elemental Analyzer at the Microanalytical Laboratory of the University of Vienna. The compounds were purified by preparative RP-HPLC using a Waters XBridge C18 column on an Agilent 1200 Series system. Milli-Q water and acetonitrile were used as eluents with a flow rate of 17 ml min−1, unless otherwise stated.
4
Comprehensive Analytical Characterization
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Elemental analyses were carried out in a Carlo-Erba microanalyser at the Microanalytical Laboratory of the University of Vienna. Electrospray ionisation mass spectrometry (ESI MS) was carried out with amaZon speed ETD Bruker instrument (Bruker Daltonik GmbH, Bremen, Germany, m/z range 0–900, ion positive/negative mode, 180 °C, heating gas N2 (5 L/min), Capillary 4500 V, End Plate Offset 500 V). UV–Vis spectra were measured on Perkin Elmer UV/Vis spectrophotometer Lambda 35. IR spectra were reported on a Bucker Vertex 70 Fourier transform IR spectrometer (4000–400 cm−1) using the ATR technique. 1D (1H, 13C) and 2D (1H-1H COSY, 1H-1H TOCSY, 1H-1H NOESY, 1H-13C HSQC, 1H-13C HMBC, 1H-15N HSQC, 1H-15N HMBC) NMR spectra were measured on a Bruker AV NEO 500 or AV III 600 spectrometers (Bruker BioSpin GmbH, Rheinstetten, Germany) in DMSO-d6 at 25 °C at NMR spectroscopy Centre of the Faculty of Chemistry of the University of Vienna.
5
Structural Characterization of Mtr4-KOW Interactions
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For all NMR measurements 5% D2O was added to the samples for locking. All spectra were recorded at 298 K on AVIII 600, AVIII 900, and AVIII 950 Bruker NMR spectrometers equipped with cryogenic triple resonance-gradient probes. For data processing, Topspin 3.5 was used while analysis was done with Sparky 3.115 (T.D. Goddard and D.G. Kneller, Sparky 3, University of California, San Francisco). HNCACB, HNCA, and HNcoCA experiments (Sattler et al. 1999 ) were recorded for protein backbone assignment as well as hetNOE data on an ∼200 µM 15N13C labeled Mtr4–KOW sample. RNAs were analyzed using 1D and 1H,1H-NOESY experiments. All samples were buffer exchanged prior to measurement to 20 mM Hepes/NaOH pH 6.5, 150 mM NaCl, 2 mM β-mercaptoethanol and 5% (v/v) glycerol. For titration experiments the protein concentration was adjusted to 15–35 µM and titrated with RNAs and Nop53 peptide as follows: The ratios used for double-stranded RNA were 1:0, 1:2, 1:5, 1:10; for Phe-tRNA 1:0, 1:2, 1:5, 1:7; and for the peptide 1:0, 1:2, 1:5, 1:10, 1:20. The dsRNA was furthermore added in a 1:7 ratio to the KOW–Nop53 peptide complex sample. The chemical shift perturbations were calculated as CSP (ppm) = [(ΔH)2 + ((ΔN)/6.51)2]0.5.
6
NMR and HPLC-MS Characterization of Compounds
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Optical rotations were obtained on a JASCO P-2000 polarimeter (Hachioji, Tokyo). UV spectra (MeOH) were measured on a Hitachi U-2900 double-beam spectrophotometer (Hitachi, Japan). Electron circular dichroic (CD) spectra (MeOH) were measured on a JASCO J-720 spectropolarimeter (Hachioji, Tokyo). NMR spectra were recorded by Bruker AV-400, and AV III-600 (CD3OD, δH 3.30 and δC 49.0 ppm). HPLC-SPE-NMR (600 MHz), composed of an Agilent 1100 liquid chromatograph (Waldbronn, Germany), a Phenomenex Prodigy ODS3 (C-18) 100 Å (250 × 4.6 mm, 5 μm) column, coupled with a diode array detector (DAD, G1315A) and a Knauer K120 HPLC pump (makeup pump), a Prospekt 2 automated solid-phase extraction unit (Spark Holland, Emmen, Holland), containing 192 HySphere resin GP cartridges (10 × 2 mm, 10–12 μm), connecting to a Gilson Liquid Handler 215 automated tube transfer (TT) system (Gilson, Inc., Middleton, WI, USA), and a Bruker AV III-600 spectrometer. HPLC-ESIMS (electrospray ionization mass spectrometry) was performed on an Agilent 1100 series liquid chromatograph, followed by an Esquire 2000 mass spectrometer (Bruker Daltonics, Germany). TLC analysis was carried out on silica gel plates (KG60-F254, Merck).
7
Multimodal Characterization Workflow
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SEC analysis was performed
using a Varian 390-LC MDS system equipped with a PL-AS RT/MT autosampler,
a PL-gel 3 μm (50 × 7.5 mm) guard column, two PL-gel 5
μm (300 × 7.5 mm) mixed-D columns using DMF with 5 mM NH4BF4 at 50 °C as eluent at a flow rate of 1.0
mL.min–1. The SEC system was equipped with ultraviolet
(UV)/visible (set at 280 and 461 nm) and differential refractive index
(DRI) detectors. Narrow molecular weight PMMA standard (200–1.0
× 106 g mol–1) were used for calibration
using a second order polynomial fit. NMR spectroscopy (1H, 13C) was conducted on a Bruker DPX-300, Bruker DRX-500
or Bruker AV III 600 spectrometer using deuterated chloroform or deuterated
methanol as solvent. All chemical shifts are reported in ppm (δ)
relative to the solvent used. FTIR spectra were acquired using a Bruker
Vector 22 FTIR spectrometer with a Golden Gate diamond attenuated
total reflection cell. A total of 64 scans were collected on samples
in their native state. Microscopy was performed using a Zeiss LSM
880 microscope. SYTO-9 dye was imaged by excitation at 488 nm and
emission at 530 nm for green fluorescence. Propidium iodide was imaged
by excitation at 561 nm and emission at 646 nm for red fluorescence.
using a Varian 390-LC MDS system equipped with a PL-AS RT/MT autosampler,
a PL-gel 3 μm (50 × 7.5 mm) guard column, two PL-gel 5
μm (300 × 7.5 mm) mixed-D columns using DMF with 5 mM NH4BF4 at 50 °C as eluent at a flow rate of 1.0
mL.min–1. The SEC system was equipped with ultraviolet
(UV)/visible (set at 280 and 461 nm) and differential refractive index
(DRI) detectors. Narrow molecular weight PMMA standard (200–1.0
× 106 g mol–1) were used for calibration
using a second order polynomial fit. NMR spectroscopy (1H, 13C) was conducted on a Bruker DPX-300, Bruker DRX-500
or Bruker AV III 600 spectrometer using deuterated chloroform or deuterated
methanol as solvent. All chemical shifts are reported in ppm (δ)
relative to the solvent used. FTIR spectra were acquired using a Bruker
Vector 22 FTIR spectrometer with a Golden Gate diamond attenuated
total reflection cell. A total of 64 scans were collected on samples
in their native state. Microscopy was performed using a Zeiss LSM
880 microscope. SYTO-9 dye was imaged by excitation at 488 nm and
emission at 530 nm for green fluorescence. Propidium iodide was imaged
by excitation at 561 nm and emission at 646 nm for red fluorescence.
8
Multi-Dimensional NMR and Mass Spectrometry
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1H NMR, 13C NMR (DEPTQ), 19F-NMR, and 2D NMR spectra were recorded
in CDCl3 or DMSO-d6 (Merck
KGaA, Darmstadt, Germany) on Bruker AV NEO 400, AV NEO 500 WB, AV
III 600 or AV III HD 700 spectrometers (Bruker, Mannheim, Germany).
Spectra evaluation was performed using MestReNova 14.2 software (Mestrelab
Research S.L., Santiago de Compostela, Spain).
Full-scan high-resolution
mass spectra (m/z 50–1600)
of the compounds dissolved in MeCN/MeOH and 1% H2O were
obtained by direct infusion measurements on a maXis ESI-Qq-TOF mass
spectrometer (Bruker, Mannheim, Germany). The sum formulas of the
detected ions were determined using Compass DataAnalysis 4.0 (Bruker,
Mannheim, Germany) based on the mass accuracy (Δm/z ≤ 5 ppm) and isotopic pattern matching
(SmartFormula algorithm).
Compound characterization data is
provided in the Supporting Information
(Figures S10–S19 ).
in CDCl3 or DMSO-d6 (Merck
KGaA, Darmstadt, Germany) on Bruker AV NEO 400, AV NEO 500 WB, AV
III 600 or AV III HD 700 spectrometers (Bruker, Mannheim, Germany).
Spectra evaluation was performed using MestReNova 14.2 software (Mestrelab
Research S.L., Santiago de Compostela, Spain).
Full-scan high-resolution
mass spectra (m/z 50–1600)
of the compounds dissolved in MeCN/MeOH and 1% H2O were
obtained by direct infusion measurements on a maXis ESI-Qq-TOF mass
spectrometer (Bruker, Mannheim, Germany). The sum formulas of the
detected ions were determined using Compass DataAnalysis 4.0 (Bruker,
Mannheim, Germany) based on the mass accuracy (Δm/z ≤ 5 ppm) and isotopic pattern matching
(SmartFormula algorithm).
Compound characterization data is
provided in the Supporting Information
(
9
Electrochemical Reduction of CO on OD-Cu
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The electrochemical reduction of CO on OD-Cu in this work was conducted in the SEIRAS spectrochemical cell shown in Fig. 1a . The OD-Cu film on a copper foil substrate was used as the working electrode, and a graphite rod and a saturated Ag/AgCl were used as the counter and reference electrodes, respectively. Before the reaction, the electrolyte in the cathode compartment was first purged with Ar, during which the pre-reduction of Cu2O to OD-Cu was conducted under −0.4 V vs. RHE. The feeding gas was then switched to CO and continuously bubbled into the electrolyte for 0.5 h to reach saturation. Then the cell was sealed, and the reaction was conducted for 10 C of charge under −0.7 V vs. RHE in 0.05 M K2CO3 and 0.1 M KOH as shown in Supplementary Fig. 13 . After the reaction, the gas products were detected by a GC (Agilent Technologies 7890B) equipped with a Flame Ionization Detector (FID) and Temperature Conductivity Detector (TCD). The liquid products were analyzed by NMR spectroscopy (Bruker AVIII 600) through an integrated peak area ratio with a 4 ppm DMSO/D2O internal standard.
10
Isotopic Labeling for 13C NMR Analysis
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13C NMR spectra were
collected on a Bruker AV-III-600 (150.9
MHz 13C frequency) at 25 °C. Samples were prepared
with 1.6 mM of the S13CN labeled protein, 8 mM ligands,
and 50 mM potassium phosphate (pH 7.0) in water. A sealed capillary
tube containing 1 M acetone in D2O was inserted into the
NMR tube that holds the protein sample. This provided both a locked
solvent and an internal standard. Chemical shifts were also checked
with an external standard of tetramethylsilane. Spectral data were
acquired for ∼3000–4000 scans. The 1D 13C
NMR spectral data obtained for each sample were compared with its
corresponding 13C DEPT 45° (distortionless enhancement
by polarization transfer) data to confirm the identity of the assigned
peaks. Under the same experimental conditions, we were unable to detect
the 13C NMR signals corresponding to the SCN probes for
samples containing either the nonisotopically enriched SCN label or
the unlabeled proteins.
collected on a Bruker AV-III-600 (150.9
MHz 13C frequency) at 25 °C. Samples were prepared
with 1.6 mM of the S13CN labeled protein, 8 mM ligands,
and 50 mM potassium phosphate (pH 7.0) in water. A sealed capillary
tube containing 1 M acetone in D2O was inserted into the
NMR tube that holds the protein sample. This provided both a locked
solvent and an internal standard. Chemical shifts were also checked
with an external standard of tetramethylsilane. Spectral data were
acquired for ∼3000–4000 scans. The 1D 13C
NMR spectral data obtained for each sample were compared with its
corresponding 13C DEPT 45° (distortionless enhancement
by polarization transfer) data to confirm the identity of the assigned
peaks. Under the same experimental conditions, we were unable to detect
the 13C NMR signals corresponding to the SCN probes for
samples containing either the nonisotopically enriched SCN label or
the unlabeled proteins.
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