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Molecules 2016, 21(7), 804; doi:10.3390/molecules21070804

Spectroscopic and Kinetic Characterization of Peroxidase-Like π-Cation Radical Pinch-Porphyrin-Iron(III) Reaction Intermediate Models of Peroxidase Enzymes

1
Centro de Química Instituto de Ciencias, Benemérita Universidad Autónoma de Puebla. Edificio 103H, Ciudad Universitaria, Col. Jardines de San Manuel, Puebla, Pue. 72570, Mexico
2
Instituto Politécnico Nacional, ESFM, Ave. Instituto Politécnico Nacional S/N, Edif. 9 U.P. Zacatenco, Col. San Pedro Zacatenco, México City 07738, Mexico
*
Author to whom correspondence should be addressed.
Academic Editors: Jose M. Palomo and Chris Frost
Received: 29 April 2016 / Revised: 1 June 2016 / Accepted: 13 June 2016 / Published: 27 June 2016
(This article belongs to the Special Issue Biomolecules Modification)
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Abstract

The spectroscopic and kinetic characterization of two intermediates from the H2O2 oxidation of three dimethyl ester [(proto), (meso), (deuteroporphyrinato) (picdien)]Fe(III) complexes ([FePPPic], [FeMPPic] and [FeDPPic], respectively) pinch-porphyrin peroxidase enzyme models, with s = 5/2 and 3/2 Fe(III) quantum mixed spin (qms) ground states is described herein. The kinetic study by UV/Vis at λmax = 465 nm showed two different types of kinetics during the oxidation process in the guaiacol test for peroxidases (13 + guaiacol + H2O2 → oxidation guaiacol products). The first intermediate was observed during the first 24 s of the reaction. When the reaction conditions were changed to higher concentration of pinch-porphyrins and hydrogen peroxide only one type of kinetics was observed. Next, the reaction was performed only between pinch-porphyrins-Fe(III) and H2O2, resulting in only two types of kinetics that were developed during the first 0–4 s. After this time a self-oxidation process was observed. Our hypotheses state that the formation of the π-cation radicals, reaction intermediates of the pinch-porphyrin-Fe(III) family with the ligand picdien [N,N’-bis-pyridin-2-ylmethyl-propane-1,3-diamine], occurred with unique kinetics that are different from the overall process and was involved in the oxidation pathway. UV-Vis, 1H-NMR and ESR spectra confirmed the formation of such intermediates. The results in this paper highlight the link between different spectroscopic techniques that positively depict the kinetic traits of artificial compounds with enzyme-like activity. View Full-Text
Keywords: pinch-porphyrins; peroxidases models; π-cation radical; spectroscopic studies pinch-porphyrins; peroxidases models; π-cation radical; spectroscopic studies
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Hernández Anzaldo, S.; Arroyo Abad, U.; León García, A.; Ramírez Rosales, D.; Zamorano Ulloa, R.; Reyes Ortega, Y. Spectroscopic and Kinetic Characterization of Peroxidase-Like π-Cation Radical Pinch-Porphyrin-Iron(III) Reaction Intermediate Models of Peroxidase Enzymes. Molecules 2016, 21, 804.

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