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Vanadium Complexes as Prospective Therapeutics: Structural Characterization of a V IV Lysozyme Adduct
Author(s) -
Santos Marino F. A.,
Correia Isabel,
Oliveira Ana R.,
Garribba Eugenio,
Pessoa João Costa,
SantosSilva Teresa
Publication year - 2014
Publication title -
european journal of inorganic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.667
H-Index - 136
eISSN - 1099-0682
pISSN - 1434-1948
DOI - 10.1002/ejic.201402408
Subject(s) - chemistry , lysozyme , covalent bond , crystallography , vanadium , adduct , electron paramagnetic resonance , side chain , stereochemistry , inorganic chemistry , nuclear magnetic resonance , organic chemistry , biochemistry , physics , polymer
The biological activity of vanadium complexes, namely, as insulin enhancers, is well known. We report a combined X‐ray crystallography, electron paramagnetic resonance, and density functional theory study of the interaction of vanadium picolinate complexes with hen egg white lysozyme (HEWL). We show that the V IV O(pic) 2 complex covalently binds to the COO – group of the side chain of Asp52 of HEWL. The long V IV =O bond obtained in the X‐ray study is explained to be due to reduction of V IV to V III during exposure of the crystals to the intense X‐ray beam.