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Models of Oxovanadium( IV )–Protein Interactions: The First Oxovanadium( IV ) Complexes with Dipeptides
Author(s) -
Tasiopoulos Anastasios J.,
Vlahos Antonis T.,
Keramidas Anastasios D.,
Kabanos Themistoklis A.,
Deligiannakis Yiannis G.,
Raptopoulou Catherine P.,
Terzis Aris
Publication year - 1996
Publication title -
angewandte chemie international edition in english
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 0570-0833
DOI - 10.1002/anie.199625311
Subject(s) - dipeptide , chemistry , carboxylate , deprotonation , amide , salt (chemistry) , nitrogen atom , sulfur , glycine , stereochemistry , medicinal chemistry , atom (system on chip) , peptide , ion , amino acid , group (periodic table) , organic chemistry , biochemistry , computer science , embedded system
The sulfur atom, the nitrogen atom of the deprotonated amide functionality, and an oxygen atom of the carboxylate group are the ligating atoms of the dipeptide N ‐(2‐mercaptopropionyl)glycine (H 3 mpg) in its complex with the VO 2+ center in the anion of 1 (shown on the right). This complex salt is accessible from [VOCl 2 (phen)] (phen = 1,10‐phenanthroline) and H 3 mpg in the presence of Et 3 N. This study provides insight into the mode of binding of a dipeptide to an oxovanadium( IV ) unit.