Disproportionation of H<sub>2</sub>O<sub>2</sub> Mediated by Diiron-Peroxo Complexes as Catalase Mimics

Heme iron and nonheme dimanganese catalases protect biological systems against oxidative damage caused by hydrogen peroxide. Rubrerythrins are ferritine-like nonheme diiron proteins, which are structurally and mechanistically distinct from the heme-type catalase but similar to a dimanganese KatB enz...

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Main Authors:	Dóra Lakk-Bogáth, Patrik Török, Flóra Viktória Csendes, Soma Keszei, Beatrix Gantner, József Kaizer
Format:	Article
Language:	English
Published:	MDPI AG 2021-07-01
Series:	Molecules
Subjects:	catalase mimics peroxide diiron-peroxo complexes structure/activity kinetic studies
Online Access:	https://www.mdpi.com/1420-3049/26/15/4501

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record_format	Article
spelling	doaj-018984a62a164b239244513a8f1f40512021-08-06T15:28:56ZengMDPI AGMolecules1420-30492021-07-01264501450110.3390/molecules26154501Disproportionation of H<sub>2</sub>O<sub>2</sub> Mediated by Diiron-Peroxo Complexes as Catalase MimicsDóra Lakk-Bogáth0Patrik Török1Flóra Viktória Csendes2Soma Keszei3Beatrix Gantner4József Kaizer5Research Group of Bioorganic and Biocoordination Chemistry, University of Pannonia, H-8201 Veszprém, HungaryResearch Group of Bioorganic and Biocoordination Chemistry, University of Pannonia, H-8201 Veszprém, HungaryResearch Group of Bioorganic and Biocoordination Chemistry, University of Pannonia, H-8201 Veszprém, HungaryResearch Group of Bioorganic and Biocoordination Chemistry, University of Pannonia, H-8201 Veszprém, HungaryResearch Group of Bioorganic and Biocoordination Chemistry, University of Pannonia, H-8201 Veszprém, HungaryResearch Group of Bioorganic and Biocoordination Chemistry, University of Pannonia, H-8201 Veszprém, HungaryHeme iron and nonheme dimanganese catalases protect biological systems against oxidative damage caused by hydrogen peroxide. Rubrerythrins are ferritine-like nonheme diiron proteins, which are structurally and mechanistically distinct from the heme-type catalase but similar to a dimanganese KatB enzyme. In order to gain more insight into the mechanism of this curious enzyme reaction, non-heme structural and functional models were carried out by the use of mononuclear [Fe<sup>II</sup>(L<sub>1–4</sub>)(solvent)<sub>3</sub>](ClO<sub>4</sub>)<sub>2</sub> (<b>1</b>–<b>4</b>) (L<sub>1</sub> = 1,3-bis(2-pyridyl-imino)isoindoline, L<sub>2</sub> = 1,3-bis(4′-methyl-2-pyridyl-imino)isoindoline, L<sub>3</sub> = 1,3-bis(4′-Chloro-2-pyridyl-imino)isoindoline, L<sub>4</sub> = 1,3-bis(5′-chloro-2-pyridyl-imino)isoindoline) complexes as catalysts, where the possible reactive intermediates, diiron-perroxo [Fe<sup>III</sup><sub>2</sub>(μ-O)(μ-1,2-O<sub>2</sub>)(L<sub>1</sub>-L<sub>4</sub>)<sub>2</sub>(Solv)<sub>2</sub>]<sup>2+</sup> (<b>5</b>–<b>8</b>) complexes are known and well-characterized. All the complexes displayed catalase-like activity, which provided clear evidence for the formation of diiron-peroxo species during the catalytic cycle. We also found that the fine-tuning of iron redox states is a critical issue, both the formation rate and the reactivity of the diiron-peroxo species showed linear correlation with the Fe<sup>III</sup>/Fe<sup>II</sup> redox potentials. Their stability and reactivity towards H<sub>2</sub>O<sub>2</sub> was also investigated and based on kinetic and mechanistic studies a plausible mechanism, including a rate-determining hydrogen atom transfer between the H<sub>2</sub>O<sub>2</sub> and diiron-peroxo species, was proposed. The present results provide one of the first examples of a nonheme diiron-peroxo complex, which shows a catalase-like reaction.https://www.mdpi.com/1420-3049/26/15/4501catalase mimicsperoxidediiron-peroxo complexesstructure/activitykinetic studies
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	Dóra Lakk-Bogáth Patrik Török Flóra Viktória Csendes Soma Keszei Beatrix Gantner József Kaizer
spellingShingle	Dóra Lakk-Bogáth Patrik Török Flóra Viktória Csendes Soma Keszei Beatrix Gantner József Kaizer Disproportionation of H<sub>2</sub>O<sub>2</sub> Mediated by Diiron-Peroxo Complexes as Catalase Mimics Molecules catalase mimics peroxide diiron-peroxo complexes structure/activity kinetic studies
author_facet	Dóra Lakk-Bogáth Patrik Török Flóra Viktória Csendes Soma Keszei Beatrix Gantner József Kaizer
author_sort	Dóra Lakk-Bogáth
title	Disproportionation of H<sub>2</sub>O<sub>2</sub> Mediated by Diiron-Peroxo Complexes as Catalase Mimics
title_short	Disproportionation of H<sub>2</sub>O<sub>2</sub> Mediated by Diiron-Peroxo Complexes as Catalase Mimics
title_full	Disproportionation of H<sub>2</sub>O<sub>2</sub> Mediated by Diiron-Peroxo Complexes as Catalase Mimics
title_fullStr	Disproportionation of H<sub>2</sub>O<sub>2</sub> Mediated by Diiron-Peroxo Complexes as Catalase Mimics
title_full_unstemmed	Disproportionation of H<sub>2</sub>O<sub>2</sub> Mediated by Diiron-Peroxo Complexes as Catalase Mimics
title_sort	disproportionation of h<sub>2</sub>o<sub>2</sub> mediated by diiron-peroxo complexes as catalase mimics
publisher	MDPI AG
series	Molecules
issn	1420-3049
publishDate	2021-07-01
description	Heme iron and nonheme dimanganese catalases protect biological systems against oxidative damage caused by hydrogen peroxide. Rubrerythrins are ferritine-like nonheme diiron proteins, which are structurally and mechanistically distinct from the heme-type catalase but similar to a dimanganese KatB enzyme. In order to gain more insight into the mechanism of this curious enzyme reaction, non-heme structural and functional models were carried out by the use of mononuclear [Fe<sup>II</sup>(L<sub>1–4</sub>)(solvent)<sub>3</sub>](ClO<sub>4</sub>)<sub>2</sub> (<b>1</b>–<b>4</b>) (L<sub>1</sub> = 1,3-bis(2-pyridyl-imino)isoindoline, L<sub>2</sub> = 1,3-bis(4′-methyl-2-pyridyl-imino)isoindoline, L<sub>3</sub> = 1,3-bis(4′-Chloro-2-pyridyl-imino)isoindoline, L<sub>4</sub> = 1,3-bis(5′-chloro-2-pyridyl-imino)isoindoline) complexes as catalysts, where the possible reactive intermediates, diiron-perroxo [Fe<sup>III</sup><sub>2</sub>(μ-O)(μ-1,2-O<sub>2</sub>)(L<sub>1</sub>-L<sub>4</sub>)<sub>2</sub>(Solv)<sub>2</sub>]<sup>2+</sup> (<b>5</b>–<b>8</b>) complexes are known and well-characterized. All the complexes displayed catalase-like activity, which provided clear evidence for the formation of diiron-peroxo species during the catalytic cycle. We also found that the fine-tuning of iron redox states is a critical issue, both the formation rate and the reactivity of the diiron-peroxo species showed linear correlation with the Fe<sup>III</sup>/Fe<sup>II</sup> redox potentials. Their stability and reactivity towards H<sub>2</sub>O<sub>2</sub> was also investigated and based on kinetic and mechanistic studies a plausible mechanism, including a rate-determining hydrogen atom transfer between the H<sub>2</sub>O<sub>2</sub> and diiron-peroxo species, was proposed. The present results provide one of the first examples of a nonheme diiron-peroxo complex, which shows a catalase-like reaction.
topic	catalase mimics peroxide diiron-peroxo complexes structure/activity kinetic studies
url	https://www.mdpi.com/1420-3049/26/15/4501
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Disproportionation of H<sub>2</sub>O<sub>2</sub> Mediated by Diiron-Peroxo Complexes as Catalase Mimics

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