Ebbe Nordlander
Professor
An Unsymmetric Ligand with a N5O2 Donor Set and Its Corresponding Dizinc Complex : A Structural and Functional Phosphoesterase Model
Author
Summary, in English
To mimic the active sites of the hydrolytic enzyme zinc phosphotriesterase, a new dinucleating unsymmetric ligand, PICIMP (2-([2-hydroxy-5-methyl-3-(([(1-methyl-1H-imidazol-2-yl)methyl](pyridin-2-ylmethyl)amino)methyl)benzyl][(1-methyl-1H-imidazol-2-yl)methyl]amino)acetic acid), has been synthesized and characterized. The hydrolytic efficacy of the complex solution (PICIMP/ZnCl2 = 1:2) has been investigated using bis-(2,4-dinitrophenyl)phosphate (BDNPP), a DNA analogue substrate. Speciation studies were undertaken by potentiometric titrations at varying pH for both the ligand and the corresponding dizinc complex to elucidate the formation of the active hydrolysis catalyst; these studies reveal that the dinuclear zinc(II) complexes, [Zn2(PICIMP)]2+ and [Zn2(PICIMP)(OH)]+ predominate in solution above pH 4. The obtained pKa of 7.44 for the deprotonation of water suggests formation of a bridging hydroxide between the two ZnII ions. Kinetic investigations of BDNPP hydrolysis over the pH range 5.5-10.5 have been performed. The cumulative results indicate the hydroxo-bridged dinuclear ZnII complex [Zn2(PICIMP)(μ-OH)]+ as the effective catalyst. Density functional theory calculations were performed to investigate the detailed reaction mechanism. The calculations suggest that the bridging hydroxide becomes terminally coordinated to one of the zinc ions before performing the nucleophilic attack in the reaction.
Department/s
- Chemical Physics
Publishing year
2018
Language
English
Pages
3986-3986
Publication/Series
European Journal of Inorganic Chemistry
Volume
2018
Issue
36
Document type
Journal article
Publisher
John Wiley & Sons Inc.
Topic
- Inorganic Chemistry
Keywords
- Active sites
- Coordination chemistry
- Metalloenzymes
- Phosphoester hydrolysis
Status
Published
ISBN/ISSN/Other
- ISSN: 1434-1948