Full-text resources of PSJD and other databases are now available in the new Library of Science.
Visit https://bibliotekanauki.pl
Preferences help
enabled [disable] Abstract
Number of results

Results found: 1

Number of results on page
first rewind previous Page / 1 next fast forward last

Search results

help Sort By:

help Limit search:
first rewind previous Page / 1 next fast forward last
EN
Although a minor constituent of cell and tissues, sulfur is an essential element to fulfil a wide range of biological processes, and it is present in the functional groups of many biomolecules that participate to redox reactions in vivo. Cysteine, one of the two S-containing aminoacids present in proteins, contains sulfur in fully reduced form and its thiol group can undergo a range of reactions under physiological conditions. X-ray absorption spectroscopy represents a unique tool to speciate the redox state of sulfur in biomolecules because of the known strong correlation between oxidation state and absorption edge energy shift (over 10 eV). Moreover, a rich X-ray absorption near edge structure is related to the chemical structures of S-containing biomolecules, as well as significant spectral changes due to biochemical action. The formation of a disulfide bond, i.e. a covalent linkage between the S atoms of two cysteine residues, or its reduction were investigated only indirectly in biomolecules. X-ray absorption spectroscopy experiments at the sulfur K-edge were performed at the soft X-ray beamline in Frascati using the wiggler source of the 0.51 GeV storage ring DAΦNE. X-ray absorption near edge structure data were collected to distinguish in situ between S-thiol and disulfide on model protein systems. Such preliminary results confirm this technique as a unique probe of sulfur chemistry in vivo. Quantitative speciation of S-metabolites can be foreseen in biological tissues with no chemical manipulations of the specimen.
first rewind previous Page / 1 next fast forward last
JavaScript is turned off in your web browser. Turn it on to take full advantage of this site, then refresh the page.