Monoesterase activity of a purple acid phosphatase mimic with a cyclam platform |
| |
Authors: | Comba Peter Gahan Lawrence R Hanson Graeme R Mereacre Valeriu Noble Christopher J Powell Annie K Prisecaru Ion Schenk Gerhard Zajaczkowski-Fischer Marta |
| |
Institution: | 1. Anorganisch‐Chemisches Institut, Universit?t Heidelberg, INF 270, 69120 Heidelberg (Germany), Fax: (+49)?6221‐546617;2. School of Chemistry and Molecular Biosciences, The University of Queensland, Brisbane, Queensland 4072 (Australia);3. Centre for Advanced Imaging, The University of Queensland, Brisbane, Queensland 4072 (Australia);4. Institut für Anorganische Chemie, Karlsruher Institut für Technologie, Engesserstrasse 15, 76131 Karlsruhe (Germany);5. National Institute for Materials Physics, Magnetism Laboratory, Bucharest (Romania);6. Department of Chemistry, National University of Ireland – Maynooth, Maynooth, Co. Kildare (Ireland) |
| |
Abstract: | The synthesis and characterization of a novel dinucleating ligand L (L=4,11-dimethyl-1,8-bis{2-N-(di-2-pyridylmethyl)amino]ethyl}cyclam) and its μ-oxo-bridged diferric complex (H(2)L){Fe(III)(2)(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. |
| |
Keywords: | bioinorganic chemistry enzymes hydrogen bonds hydrolysis iron |
本文献已被 PubMed 等数据库收录! |
|