Ein Hämerythrin‐Modellkomplex mit Katalaseaktivität

Mauerer, Bert; Crane, Jonathan D.; Schuler, Jürgen; Wieghardt, Karl; Nuber, Bernhard

doi:10.1002/ange.19931050238

Cited by 4 publications

(2 citation statements)

References 15 publications

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“…Disproportionation of H 2 O 2 into O 2 and H 2 O has been reported to occur upon reaction of H 2 O 2 with a synthetic Hr model complex. 18 We found that the met-WT reacted with H 2 O 2 within 10 min with a concomitant evolution of O 2 , which was confirmed by gas chromatography (Fig. S4, ESI † ).…”

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confidence: 61%

H₂O₂-dependent substrate oxidation by an engineered diiron site in a bacterial hemerythrin

et al. 2014

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supporting

confidence: 61%

H₂O₂-dependent substrate oxidation by an engineered diiron site in a bacterial hemerythrin

et al. 2014

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“…Several porphyrin-based Fe III complexes and Fe(II/III) complexes of non-heme ligands have been prepared in the past and claimed to be catalase mimics. However, none of these compounds satisfies the above definition in all aspects. ,,,, …”

Section: Discussionmentioning

confidence: 99%

Fe^III Complexes of 1,4,8,11-Tetraaza[14]annulenes as Catalase Mimics

et al. 2007

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The development of enzyme mimics of catalase which decompose hydrogen peroxide to water and molecular oxygen according to the 2:1 stoichiometry of native catalase and in aqueous solution at pH 7 and at micromolar concentrations of the enzyme model and hydrogen peroxide is reported. For this purpose, iron(III) complexes of 1,4,8,11-tetraaza[14]annulenes are prepared by various procedures. Efficacious preparations utilize reaction of the [N4] macrocyles with FeII salts in the presence of triphenylamine, followed by gentle oxidation of the FeII complexes by molecular oxygen or by tris(4-bromophenyl)aminium hexachloroantimonate. The complexes are characterized by SQUID magnetometry and by Mössbauer, EPR, and UV/vis spectrometry. In the solid state, the iron(III) center of the catalytically active complexes exists in the intermediate (quartet, S = 3/2) spin state. Several of these complexes decompose hydrogen peroxide in aqueous buffer solution at pH 7.2 at room temperature with turnover numbers between 40 and 80. The apparent second-order rate constant for hydrogen peroxide decomposition is in the range of 1400-2400 M(-1) s(-1), about 3 orders of magnitude lower than the value for native catalase. Besides oxygen production, a non-oxygen releasing pathway of hydrogen peroxide decomposition is unveiled.

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Ein Modell für Semimet‐Hämerythrin; NMR‐spektroskopischer Nachweis für die Lokalisierung der Ladung in Bis(μ‐carboxylato)‐(μ‐phenolato)dieisen(II,III)‐Komplexen in Lösung

et al. 1995

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ZUSCHRIFTEN dung dieses partiell delokalisierten Anions wird die Spaltung der P-Ph-Bindung im zweiten Schritt, der zu 6 fiihrt, ausgeschlossen. Die Anionen von 6 lassen sich anhand ihrer tieffeldverschobenen 31P-NMR-Signale (6 = 152-206) und ihrer grolJen Kopplungskonstanten 'J(P,P) und 2J(P,H) von ca. 440 bzw. 37 Hz identifizieren; diese Merkmale sind charakteristisch fur Polyphospholid-Ionen [']. Als weiterer Nachweis diente die 6 b Synthese des 1,2-Diphosphaferrocens 7 aus 6 b. ExperimentellesAlle Reaktionen wurden unter Argon durchgefuhrt. Die Losungsmittel wurden mit Standardmethoden gereinigt uud getrocknet. Die Syuthesen der als Ausgangsverbindungen verwendeten Titanacyclobutene wurden nach Lit. [12,13] durchgefuhrt.

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Ein Hämerythrin‐Modellkomplex mit Katalaseaktivität

Cited by 4 publications

References 15 publications

H₂O₂-dependent substrate oxidation by an engineered diiron site in a bacterial hemerythrin

H₂O₂-dependent substrate oxidation by an engineered diiron site in a bacterial hemerythrin

Fe^III Complexes of 1,4,8,11-Tetraaza[14]annulenes as Catalase Mimics

Ein Modell für Semimet‐Hämerythrin; NMR‐spektroskopischer Nachweis für die Lokalisierung der Ladung in Bis(μ‐carboxylato)‐(μ‐phenolato)dieisen(II,III)‐Komplexen in Lösung

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Ein Hämerythrin‐Modellkomplex mit Katalaseaktivität

Cited by 4 publications

References 15 publications

H2O2-dependent substrate oxidation by an engineered diiron site in a bacterial hemerythrin

H2O2-dependent substrate oxidation by an engineered diiron site in a bacterial hemerythrin

FeIII Complexes of 1,4,8,11-Tetraaza[14]annulenes as Catalase Mimics

Ein Modell für Semimet‐Hämerythrin; NMR‐spektroskopischer Nachweis für die Lokalisierung der Ladung in Bis(μ‐carboxylato)‐(μ‐phenolato)dieisen(II,III)‐Komplexen in Lösung

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H₂O₂-dependent substrate oxidation by an engineered diiron site in a bacterial hemerythrin

H₂O₂-dependent substrate oxidation by an engineered diiron site in a bacterial hemerythrin

Fe^III Complexes of 1,4,8,11-Tetraaza[14]annulenes as Catalase Mimics