Abstract:
X-ray Absorption Near Edge Structure (XANES) spectroscopy, often provides a direct correlation between observed resonances in the spectrum and molecular bonds in the sample. This can be used as a fingerprint for the presence of a given molecular environment of the absorber atom in a sample. As the white line is found at similar energy positions for S-C and S-H bonds, this approach is impossible when both types of bond are present simultaneously, as often in biological systems. To develop a criterium for the presence of S-H bonds in such samples, reduced glutathione, reduced coenzyme A, cysteine and their corresponding oxidized forms were investigated using sulfur K-edge XANES, revealing a unique feature at 2 475.8 eV in the respective difference spectra. To correlate this structure to S-H bonds, H2S and H2S2 were measured, whose difference spectrum also shows a structure at this energy position, whereas it is not present throughout a variety of C-S-C/C-S-S-C environments. Theoretical investigations suggest its correlation to a Rydberg transition occurring in the case of a S-H bond. Using this criterium, the presence of S-H bonds is in the purple sulfur bacterium Allochromatium vinosum during oxidation of intracellular accumulated sulfur, is proved, as expected from biological considerations.
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Received 1st February 2002 / Received in final form 10 June 2002 Published online 13 September 2002
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Prange, A., Dahl, C., Trüper, H. et al. Investigation of S-H bonds in biologically important compounds by sulfur K-edge X-ray absorption spectroscopy. Eur. Phys. J. D 20, 589–596 (2002). https://doi.org/10.1140/epjd/e2002-00156-5
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DOI: https://doi.org/10.1140/epjd/e2002-00156-5