Abstract
Elucidation of the structure and function of biomolecules provides us knowledge that can be transferred into the generation of new materials and eventually applications in e.g., catalysis or bioassays. The main problems, however, concern the complexity of the natural systems and their limited availability, which necessitates utilization of simple biomimetic analogues that are, to a certain degree, similar in terms of structure and thus behaviour. We have, therefore, devised a small library of six tridentate N-heterocyclic coordinating agents (L1–L6), which, upon complexation, form two groups of artificial, monometallic non-heme iron species. Utilization of iron(III) chloride leads to the formation of the 1:1 (Fe:Ln) ‘open’ complexes, whereas iron(II) trifluoromethanosulfonate allows for the synthesis of 1:2 (M:Ln) ‘closed’ systems. The structural differences between the individual complexes are a result of the information encoded within the metallic centre and the chosen counterion, whereas the organic scaffold influences the observed properties. Indeed, the number and nature of the external hydrogen bond donors coming from the presence of (benz)imidazole moieties in the ligand framework are responsible for the observed biological behaviour in terms of mimicking phenoxazinone synthase activity and interaction with DNA.
Highlights
Nature exhibits an astonishing ability to construct sophisticated molecular machineries to target selected, otherwise hardly approachable by synthetic chemists, molecular transformations [1].Metalloenzymes were recognized as one class of such species, with judiciously chosen transition metal ions and enzyme active sites being able to facilitate various redox processes in a catalytic and selective manner [2]
Thanks to observation of changes in the intensity of bands, it is possible to confirm the catalytic properties of the studied complexes, since blank tests without catalyst (Figure S36) confirm that the latter is necessary to obtain the observed conversion of OAPH to aminophenoxazine-3-one chromophore (APX)
Information encoded within iron(II/III) metallic centres and counterions allowed for generation of two families of complexes, which we term as ‘open’: [formation of the 1:1 (Fe)(Lx )Cl3 ] and ‘closed’:
Summary
Nature exhibits an astonishing ability to construct sophisticated molecular machineries to target selected, otherwise hardly approachable by synthetic chemists, molecular transformations [1]. The natural systems’ complexity necessitates the use of artificially constructed biomimetic analogues for further advancement of this discipline [4] This solution provides access to simple, readily accessible species that retain certain structural features of enzymes, and so their chemical behaviour and function may become mimicked. One may discriminate heme [7] and non-heme [8] Fe-based enzymes, classification, and functions that depend in nature and electronic states that favour binding of O2 [5,6]. The seminal, most widely studied examples of the heme [7] and non-heme [8] Fe-based enzymes, classification, and functions that depend on the structural former group involve studies on the families of horseradish peroxidases [9] and cytochromes P450 framework of its active site.
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