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<p>A low-molecular-weight analog of the 1-aminocyclopropane carboxylic acid oxidase (ACCO), [Tp<sup>Mes</sup>FeACC], <b>1</b>, where the (His₂Asp)iron(II) moiety is mimicked by a hydrotris(3-mesitylpyrazol-1-yl)borato iron(II) unit, to which the natural substrate aminocyclopropane carboxylate is coordinated, has been accessed and structurally characterized. It was found to react slowly with O<sub>2</sub> to yield the biological product ethylene. To create models of the intermediates proposed as part of the catalytic cycle of the ACCO <b>1</b> was treated with tBuOOH and mCPBA at low temperatures, which generated the respective Fe<sup>III</sup>OOtBu and Fe<sup>IV</sup>=O intermediates as shown by spectroscopic analysis. Studies on their behavior upon annealing reveal a non-biomimetic reactivity.</p> Graphical Abstract <p></p>

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A tris(pyrazolyl)-based model for the aminocyclopropane carboxylic acid oxidase and its behavior towards oxidants

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2025年9月12日

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  • Lars Müller,
  • Charikleia Tzatza,
  • Santina Hoof,
  • A. Jalila Simaan,
  • Christian Limberg

摘要

A low-molecular-weight analog of the 1-aminocyclopropane carboxylic acid oxidase (ACCO), [TpMesFeACC], 1, where the (His₂Asp)iron(II) moiety is mimicked by a hydrotris(3-mesitylpyrazol-1-yl)borato iron(II) unit, to which the natural substrate aminocyclopropane carboxylate is coordinated, has been accessed and structurally characterized. It was found to react slowly with O2 to yield the biological product ethylene. To create models of the intermediates proposed as part of the catalytic cycle of the ACCO 1 was treated with tBuOOH and mCPBA at low temperatures, which generated the respective FeIIIOOtBu and FeIV=O intermediates as shown by spectroscopic analysis. Studies on their behavior upon annealing reveal a non-biomimetic reactivity.

Graphical Abstract