2011
DOI: 10.1002/anie.201103981
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Crystallography Aided by Atomic Core‐Level Binding Energies: Proton Transfer versus Hydrogen Bonding in Organic Crystal Structures

Abstract: Ionic bond or hydrogen bridge? Brønsted proton transfer to nitrogen acceptors in organic crystals causes strong N1s core-level binding energy shifts. A study of 15 organic cocrystal and salt systems shows that standard X-ray photoelectron spectroscopy (XPS) can be used as a complementary method to X-ray crystallography for distinguishing proton transfer from H-bonding in organic condensed matter.

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Cited by 39 publications
(55 citation statements)
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“…A significant increase in nitrogen results from attachment of the peptide (Table ), with increased intensity at 400.1 eV (Fig. ) representative of the additional amide peptide linkages and the arginine side‐chain, while the slight asymmetry to high E B values reflects the presence of NH 3 + at the free arginine N‐terminus (Table ) . Increased intensity is also observed for amide‐specific binding energies in the C1s and O1s spectra (Fig.…”
Section: Resultsmentioning
confidence: 92%
“…A significant increase in nitrogen results from attachment of the peptide (Table ), with increased intensity at 400.1 eV (Fig. ) representative of the additional amide peptide linkages and the arginine side‐chain, while the slight asymmetry to high E B values reflects the presence of NH 3 + at the free arginine N‐terminus (Table ) . Increased intensity is also observed for amide‐specific binding energies in the C1s and O1s spectra (Fig.…”
Section: Resultsmentioning
confidence: 92%
“…A shoulder peak for N 1s is located at 401.0 eV due to protonation of NH 3 , which can be used to identify the formation of the ammonium (NH 4 + ) salt. 40 The reducing binding energies at 513.5 and 533.2 eV can be ascribed to the O atoms in —C=O and —COOH, respectively (Figure 3d). The high-resolution O 1s spectrum observed at 532.3 eV is resolved into two characteristic peaks for —C=O in H bond and —COO – in the ammonium salt.…”
Section: Resultsmentioning
confidence: 97%
“…4, Table I). A significant increase in nitrogen resulted from attachment of the peptide (Table I), with photoemission at 400.1 eV representative of the additional amide peptide linkages and the arginine side‐chain, while the slight asymmetry to high E B values reflected the presence of NH 3 + at the free arginine N‐terminus 22. The sulfur photoemission around 168.5 eV (Fig.…”
Section: Resultsmentioning
confidence: 99%