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2006 | 109 | 3 | 335-340
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X-Ray Absorption Near Edge Spectroscopy of Sulfur in Biomolecules: Two Examples from Glutathione and Insulin

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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.
Physical description
  • I.N.F.N. - Laboratori Nazionali di Frascati, via Fermi 40, 00044 Frascati, Italy
  • Department of Pathology, Section of Immunology, University of Verona Policlinico GB Rossi, P. le L.A. Scuro, 10, 37134 Verona, Italy
  • Department of Pathology, Section of Immunology, University of Verona Policlinico GB Rossi, P. le L.A. Scuro, 10, 37134 Verona, Italy
  • Department of Informatics, Faculty of Science, University of Verona, Ca' Vignal 2, 37134 Verona, Italy
  • 1. H. Sies, R. Brigelius, T.P.M. Ackerboom, in: Functions of Glutathione: Biochemical, Physiological, Toxicological, and Clinical Aspects, Eds. A. Larsson, S. Orrenius, A. Holmgren, B. Mannervik, Raven Press, New York 1983, p. 231
  • 2. H.F. Gilbert, in: Advances in Enzymology, Vol. 63, Ed. A. Meister, Wiley, New York 1990, p. 69
  • 3. J. Szpunar, Analyst, 130, 442, 2005
  • 4. E. Burattini, G. Cinque, S. Dabagov, A. Grilli, A. Marcelli, F. Monti, E. Pace, M. Piccinini, A. Raco, in: Proc. 8th Int. Conf. SRI 2003, Eds. T. Warwick, J. Arthur, H.A. Padmore, J. Stöhr, AIP Conf. Proc., San Francisco 2004, Vol. 705, p. 81
  • 5. G. Cinque, E. Burattini, A. Grilli, S. Dadagov, in: Int. Conf. on Charged and Neutral Particles Channeling Phenomena, Channeling 2004, Ed. S.B. Dabagov, SPIE Proc. 2005, Vol. 5974, INFN, Lab. Nazionali di Frascati (Italy) and RAS, P.N. Lebedev Physical Institute (Russia), 2005, p. 448
  • 6. G.P. Williams, in: X-Ray Data Booklet, Eds. A.C. Thompson, D. Vaughan, Lawrence Berkeley National Laboratory, Berkeley 2001, Sec. 1.1
  • 7. I.J. Pickering, R.C. Prince, T. Divers, G.N. George, FEBS Lett., 441, 11, 1998
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