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- Title
Vanadium Complexes as Prospective Therapeutics: Structural Characterization of a V<sup>IV</sup> Lysozyme Adduct (Eur. J. Inorg. Chem. 21/2014).
- Authors
Santos, Marino F. A.; Correia, Isabel; Oliveira, Ana R.; Garribba, Eugenio; Pessoa, João Costa; Santos ‐ Silva, Teresa
- Abstract
The cover picture shows a representation of the HEWL–VIVO(pic)2 adduct (HEWL: hen egg white lysozyme). Our X ‐ ray crystallography results show that the VIVO(pic)2 complex covalently binds to the COO– group of the side ‐ chain Asp52 residue of HEWL. Although a relatively long VIV=O bond was obtained (ca. 1.82 Å), a combined approach using EPR and DFT techniques confirms that the carboxylate group of the Asp52 residue of HEWL binds to VIVO(pic)2 and, moreover, that the oxidation state of vanadium is VIV. We conclude that the long VIV=O bond obtained is the result of the exposure of the crystals to the very intense X ‐ ray beam, which induces a progressive reduction of VIV to VIII and the concomitant bond elongation. These results may be important for the development of vanadium complexes as therapeutic agents, namely as oral insulin substitutes for the treatment of diabetes. We would like to thank Rui Pedro Bordalo for designing the cover picture. Details are discussed in the Short Communication by J. C. Pessoa, T. Santos ‐ Silva et al. on p. 3293 ff. For more on the story behind the cover research, see the Cover Profile.
- Subjects
VANADIUM; LYSOZYMES; CHEMICAL adducts; THERAPEUTICS
- Publication
European Journal of Inorganic Chemistry, 2014, Vol 2014, Issue 21, pn/a
- ISSN
1434-1948
- Publication type
Article
- DOI
10.1002/ejic.201402408