A New Heterobinuclear FeIIICuII Complex with a Single Terminal FeIII–O(phenolate) Bond. Relevance to Purple Acid Phosphatases and Nucleases

Lanznaster, Mauricio, Neves, Ademir, Bortoluzzi, Adailton J., Aires, Veronika V. E., Szpoganicz, Bruno, Terenzi, Hernan, Severino, Patricia C., Fuller, Julie M., Drew, Simon C., Gahan, Lawrence R., Hanson, Graeme R., Riley, Mark J. and Schenk, Gerhard (2005) A New Heterobinuclear FeIIICuII Complex with a Single Terminal FeIII–O(phenolate) Bond. Relevance to Purple Acid Phosphatases and Nucleases. Journal of Biological Inorganic Chemistry, 10 4: 319-332.

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Author Lanznaster, Mauricio
Neves, Ademir
Bortoluzzi, Adailton J.
Aires, Veronika V. E.
Szpoganicz, Bruno
Terenzi, Hernan
Severino, Patricia C.
Fuller, Julie M.
Drew, Simon C.
Gahan, Lawrence R.
Hanson, Graeme R.
Riley, Mark J.
Schenk, Gerhard
Title A New Heterobinuclear FeIIICuII Complex with a Single Terminal FeIII–O(phenolate) Bond. Relevance to Purple Acid Phosphatases and Nucleases
Journal name Journal of Biological Inorganic Chemistry   Check publisher's open access policy
ISSN 0949-8257
1432-1327
Publication date 2005
Sub-type Article (original research)
DOI 10.1007/s00775-005-0635-7
Volume 10
Issue 4
Start page 319
End page 332
Total pages 14
Place of publication New York
Publisher Springer
Language eng
Subject 250201 Transition Metal Chemistry
780103 Chemical sciences
250204 Bioinorganic Chemistry
Abstract A novel heterobinuclear mixed valence complex [Fe^IIICu^II(BPBPMP)(OAc)_2]ClO_4, 1, with the unsymmetrical N_5O_2 donor ligand 2-bis[{(2-pyridylmethyl)aminomethyl}-6-{(2-hydroxybenzyl)(2-pyridylmethyl)} aminomethyl]-4-methylphenol (H_2BPBPMP) has been synthesized and characterized. A combination of data from mass spectrometry, potentiometric titrations, X-ray absorption and electron paramagnetic resonance spectroscopy, as well as kinetics measurements indicates that in ethanol/water solutions an [Fe^III-(nu)OH-Cu^IIOH_2]+ species is generated which is the likely catalyst for 2,4-bis(dinitrophenyl)phosphate and DNA hydrolysis. Insofar as the data are consistent with the presence of an Fe_III-bound hydroxide acting as a nucleophile during catalysis, 1 presents a suitable mimic for the hydrolytic enzyme purple acid phosphatase. Notably, 1 is significantly more reactive than its isostructural homologues with different metal composition (Fe^IIIM^II, where M^II is Zn^II, Mn^II, Ni^II,or Fe^II). Of particular interest is the observation that cleavage of double-stranded plasmid DNA occurs even at very low concentrations of 1 (2.5 nuM), under physiological conditions (optimum pH of 7.0), with a rate enhancement of 2.7 x 10^7 over the uncatalyzed reaction. Thus, 1 is one of the most effective model complexes to date, mimicking the function of nucleases.
Keyword Biochemistry & Molecular Biology
Chemistry, Inorganic & Nuclear
Heterobinuclear (fecuii)-cu-iii Complex
Purple Acid Phosphatase
Phosphate Diester Hydrolysis
DNA cleavage
EPR
XAS
Pig Allantoic Fluid
Crystal-structure
Sweet-potato
Active-site
Angstrom Resolution
Diester Hydrolysis
Redox Properties
Epr-spectra
Metal-ions
Q-Index Code C1
Additional Notes Originally published as Mauricio Lanznaster, Ademir Neves, Adailton J. Bortoluzzi, Veronika V. E. Aires, Bruno Szpoganicz, Hernán Terenzi, Patricia Cardoso Severino2, Julie M. Fuller, Simon C. Drew, Lawrence R. Gahan, Graeme R. Hanson, Mark J. Riley and Gerhard Schenk (2005) A New Heterobinuclear FeIIICuII Complex with a Single Terminal FeIII–O(phenolate) Bond. Relevance to Purple Acid Phosphatases and Nucleases, Journal of Biological Inorganic Chemistry, 10 (4): 319-332. The original publication is available at www.springerlink.com. Copyright 2005 Springer Verlag. All rights reserved.

Document type: Journal Article
Sub-type: Article (original research)
Collections: Excellence in Research Australia (ERA) - Collection
School of Chemistry and Molecular Biosciences
 
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Created: Fri, 22 Jul 2005, 10:00:00 EST by Mark J Riley on behalf of School of Chemistry & Molecular Biosciences