A Structural and Functional Model for the 1-Aminocyclopropane-1-carboxylic Acid Oxidase - Archive ouverte HAL
Article Dans Une Revue Angewandte Chemie International Edition Année : 2015

A Structural and Functional Model for the 1-Aminocyclopropane-1-carboxylic Acid Oxidase

Résumé

The hitherto most realistic low-molecular-weight analogue for the 1-aminocyclopropane-1-carboxylic acid oxidase (ACCO) is reported. The ACCOs 2-His-1-carboxylate iron(II) active site was mimicked by a TpFe moiety, to which the natural substrate ACC could be bound. The resulting complex [Tp Me,Ph FeACC] (1), according to X-ray diffraction analysis performed for the nickel analogue,represents an excellent structural model, featuring ACC coordinated in a bidentate fashion—as proposed for the enzymatic substrate complex—as well as a vacant coordination site that forms the basis for the first successful replication also of the ACCO function: 1 is the first known ACC complex that reacts with O2 to produce ethylene. As a FeOOH species had been suggested as intermediate in the catalytic cycle,H2O2 was tested as the oxidant, too, and indeed evolution of ethylene proceeded even more rapidly to give 65 % yield.
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hal-01475561 , version 1 (02-02-2022)

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Madleen Sallmann, Fabio Oldenburg, Beatrice Braun, Marius Réglier, Ariane Jalila Simaan, et al.. A Structural and Functional Model for the 1-Aminocyclopropane-1-carboxylic Acid Oxidase. Angewandte Chemie International Edition, 2015, 54 (42), pp.12325-12328. ⟨10.1002/anie.201502529⟩. ⟨hal-01475561⟩
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