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Pentaglycine–Ni II Complex: From Kinetics to Structure
Author(s) -
Gaisin Zeev,
Gellerman Gary,
Meyerstein Dan
Publication year - 2013
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.201300039
Subject(s) - chemistry , deprotonation , amine gas treating , nickel , nucleophile , aqueous solution , reaction rate constant , peptide , kinetics , inorganic chemistry , medicinal chemistry , crystallography , stereochemistry , catalysis , organic chemistry , ion , quantum mechanics , biochemistry , physics
Binding Ni II to the terminal amine of a peptide depresses totally its nucleophilic character as measured by the rate constant of the reaction of the peptide with 4‐nitrophenyl acetate. The structure of Ni II () in aqueous solutions was determined by this technique. The results indicate that the ratio of complexes in which the nickel is bound to four deprotonated peptide nitrogen atoms to those in which the nickel is bound to the terminal amine and three deprotonated peptide nitrogen atoms increases as the pH increases. At pH 9.0, this ratio is approximately 1.