Journal
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
Volume 54, Issue 42, Pages 12325-12328Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/anie.201502529
Keywords
aminocyclopropane-1-carboxylic acid; enzyme models; iron; oxidase; oxygen
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Funding
- Humboldt-Universitat zu Berlin
- DFG
- EU-COST Network on spin state reactivity [CM1305]
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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 O-2 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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