Monoesterase activity of a purple acid phosphatase mimic with a cyclam platform

• Verfasst von: Comba, Peter [VerfasserIn]
• Verfasst von: Zajaczkowski-Fischer, Marta [VerfasserIn]
• Titel: Monoesterase activity of a purple acid phosphatase mimic with a cyclam platform
• Verf.angabe: Peter Comba, Lawrence R. Gahan, Graeme R. Hanson, Valeriu Mereacre, Christopher J. Noble, Annie K. Powell, Ion Prisecaru, Gerhard Schenk and Marta Zajaczkowski‐Fischer
• Umfang: 11 S.
• Fussnoten: Gesehen am 22.08.2018
• Titel Quelle: Enthalten in: Chemistry - a European journal
• Jahr Quelle: 2012
• Band/Heft Quelle: 18(2012), 6, S. 1700-1710
• ISSN Quelle: 1521-3765
• DOI: doi:10.1002/chem.201100229
• Datenträger: Online-Ressource
• Sprache: eng
• K10plus-PPN: 1580269613

Abstract

The synthesis and characterization of a novel dinucleating ligand L (L=4,11-dimethyl-1,8-bis2-[N-(di-2-pyridylmethyl)amino]ethylcyclam) and its μ-oxo-bridged diferric complex [(H2L)FeIII2(O)(Cl)4]2+ are reported. This diiron(III) complex is the first example of a truly functional purple acid phosphatase (PAP) mimic as it accelerates the hydrolysis of the activated phosphomonoester 2,4-dinitrophenyl phosphate (DNPP). The spectroscopic and kinetic data indicate that only substrates that are monodentately bound to one of the two ferric ions can be attacked by a suitable nucleophile. This is, most probably, a terminal iron(III)-bound hydroxide. DFT calculations support this assumption and also highlight the importance of secondary interactions, exerted by the protonated cyclam platform, for the positioning and activation of the iron(III)-bound substrate. Similar effects are postulated in the native enzyme but addressed in PAP mimics for the first time.