Accessibility navigation


Enantiospecific adsorption of alanine on the chiral Cu{531} surface

Gladys, M.J., Stevens, A.V., Scott, N.R., Jones, G., Batchelor, D. and Held, G. (2007) Enantiospecific adsorption of alanine on the chiral Cu{531} surface. Journal of Physical Chemistry C, 111 (23). pp. 8331-8336. ISSN 1932-7447

Full text not archived in this repository.

To link to this article DOI: 10.1021/jp070621f

Abstract/Summary

We have studied enantiospecific differences in the adsorption of (S)- and (R)-alanine on Cu{531}R using low-energy electron diffraction (LEED), X-ray photoelectron spectroscopy, and near edge X-ray absorption fine structure (NEXAFS) spectroscopy. At saturation coverage, alanine adsorbs as alaninate forming a p(1 4) superstructure. LEED shows a significantly higher degree of long-range order for the S than for the R enantiomer. Also carbon K-edge NEXAFS spectra show differences between (S)- and (R)-alanine in the variations of the ð resonance when the linear polarization vector is rotated within the surface plane. This indicates differences in the local adsorption geometries of the molecules, most likely caused by the interaction between the methyl group and the metal surface and/or intermolecular hydrogen bonds. Comparison with model calculations and additional information from LEED and photoelectron spectroscopy suggest that both enantiomers of alaninate adsorb in two different orientations associated with triangular adsorption sites on {110} and {311} microfacets of the Cu{531} surface. The experimental data are ambiguous as to the exact difference between the local geometries of the two enantiomers. In one of two models that fit the data equally well, significantly more (R)-alaninate molecules are adsorbed on {110} sites than on {311} sites whereas for (S)-alaninate the numbers are equal. The enantiospecific differences found in these experiments are much more pronounced than those reported from other ultrahigh vacuum techniques applied to similar systems.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
ID Code:16621
Publisher:American Chemical Society

Centaur Editors: Update this record

Page navigation