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A Structural and Functional Model for the 1‐Aminocyclopropane‐1‐carboxylic Acid Oxidase
Author(s) -
Sallmann Madleen,
Oldenburg Fabio,
Braun Beatrice,
Réglier Marius,
Simaan A. Jalila,
Limberg Christian
Publication year - 2015
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201502529
Subject(s) - chemistry , carboxylate , moiety , substrate (aquarium) , ethylene , denticity , carboxylic acid , catalytic cycle , stereochemistry , yield (engineering) , oxidase test , active site , catalysis , enzyme , crystallography , crystal structure , organic chemistry , materials science , biology , ecology , metallurgy
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, H 2 O 2 was tested as the oxidant, too, and indeed evolution of ethylene proceeded even more rapidly to give 65 % yield.