title: Utilizing the Trispyrazolyl Borate Ligand for the Mimicking of O2-Activating Mononuclear Nonheme Iron Enzymes.
abstract: Mononuclear, O2-activating nonheme iron enzymes are a fascinating class of metalloproteines, capable of realizing the most different reactions, ranging from C-H activation, via O atom transfer to C-C bond cleavage, in the course of O2 activation. They can lead us the way to achieve similar reactions with comparable efficiency and selectivity in chemical laboratories, which would be highly desirable aiming at accessing value-added products or to achieve degradation of unwanted compounds. Hence, these enyzmes motivate attempts to construct artificial low-molecular weight analogues, mimicking structural or functional characteristics. Such models can, for instance, provide insights about which of the features inherent to an active site are essential and guarantee the enzyme function, and from this kind of information the minimal requirements for a biomimetic or bioinspired complex that may be applied in catalysis can be derived. On the other hand, they can contribute to an understanding of the enzyme functioning. In order to create such replicates, it is important to faithfully mimic the surroundings of the iron centers in their active sites. Most of them feature two histidine residues and one carboxylate donor, while a few exhibit a deceptively simple (His)3Fe active site. For the simulation of these, the trispyrazolyl borate ligand (Tp) particularly offers itself, as the facial arrangement of three pyrazole donors is reminiscent of the three histidine-derived imidazole donors. The focus of this Account will be on bioinorganic/biomimetic research from our laboratory utilizing Tp ligands to develop molecular models for (i) two representatives of the (His)3Fe-enzyme family, namely, the cysteine dioxygenase (CDO) and acetyl acetone dioxygenase (Dke1), (ii) a related but less well-explored variant of the CDO-the 2-aminoethanethiol dioxygenase-as well as (iii) the 2-His-1-carboxylate representative 1-aminocyclopropane-1-carboxylic acid oxidase (ACCO). The CDO catalyzes the dioxygenation of cysteine with O2 to give cysteine sulfinic acid, which could be mimicked at TpFe units in a realistic manner. Furthermore, the successful dioxygenation of 2-aminoethanethiol at the same complex metal fragments lends further support to the hypothesis that the active sites of CDO and the one of 2-aminoethanethiol dioxygenase, whose structure is unknown, are quite similar. Dke1 is capable of cleaving diketones and ketoesters to give the corresponding carboxylic acids and α-keto aldehydes, and Tp-based models have achieved comparable C-C bond cleavage reactions. The ACCO develops ethylene from ACC in the course of oxidation, and recently this has been achieved the first time for a TpFe model, too.
authors: Humboldt-Universität zu Berlin , Department of Chemistry, Brook-Taylor-Str. 2, 12489 Berlin, Germany.
authors: Madleen
authors: M
authors: Sallmann
authors: Humboldt-Universität zu Berlin , Department of Chemistry, Brook-Taylor-Str. 2, 12489 Berlin, Germany.
authors: Christian
authors: C
authors: Limberg
mesh_terms: D032701:Biomimetics; D001881:Borates / Q000737:chemistry*; D050558:Cysteine Dioxygenase / Q000378:metabolism; D049308:Dioxygenases / Q000378:metabolism; D008024:Ligands; D011720:Pyrazoles / Q000737:chemistry*
chemical_list: D001881:Borates; D008024:Ligands; D011720:Pyrazoles; D049308:Dioxygenases; C000606529:acetyl acetone dioxygenase, Acinetobacter johnsonii; D050558:Cysteine Dioxygenase