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Site-selective formation of an iron(iv)-oxo species at the more electron-rich iron atom of heteroleptic ?-nitrido diiron phthalocyanines.

ABSTRACT: Iron(iv)-oxo species have been identified as the active intermediates in key enzymatic processes, and their catalytic properties are strongly affected by the equatorial and axial ligands bound to the metal, but details of these effects are still unresolved. In our aim to create better and more efficient oxidants of H-atom abstraction reactions, we have investigated a unique heteroleptic diiron phthalocyanine complex. We propose a novel intramolecular approach to determine the structural features that govern the catalytic activity of iron(iv)-oxo sites. Heteroleptic ?-nitrido diiron phthalocyanine complexes having an unsubstituted phthalocyanine (Pc1) and a phthalocyanine ligand substituted with electron-withdrawing alkylsulfonyl groups (PcSO₂R) were prepared and characterized. A reaction with terminal oxidants gives two isomeric iron(iv)-oxo and iron(iii)-hydroperoxo species with abundances dependent on the equatorial ligand. Cryospray ionization mass spectrometry (CSI-MS) characterized both hydroperoxo and diiron oxo species in the presence of H₂O₂. When m-CPBA was used as the oxidant, the formation of diiron oxo species (PcSO₂R)FeNFe(Pc1)[double bond, length as m-dash]O was also evidenced. Sufficient amounts of these transient species were trapped in the quadrupole region of the mass-spectrometer and underwent a CID-MS/MS fragmentation. Analyses of fragmentation patterns indicated a preferential formation of hydroperoxo and oxo moieties at more electron-rich iron sites of both heteroleptic ?-nitrido complexes. DFT calculations show that both isomers are close in energy. However, the analysis of the iron(iii)-hydroperoxo bond strength reveals major differences for the (Pc1)FeN(PcSO₂R)Fe^IIIOOH system as compared to (PcSO₂R)FeN(Pc1)Fe^IIIOOH system, and, hence binding of a terminal oxidant will be preferentially on more electron-rich sides. Subsequent kinetics studies showed that these oxidants are able to even oxidize methane to formic acid efficiently.

SUBMITTER: Isci U

PROVIDER: S-EPMC6088558 | biostudies-literature | 2015 Aug

REPOSITORIES: biostudies-literature

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Site-selective formation of an iron(iv)-oxo species at the more electron-rich iron atom of heteroleptic μ-nitrido diiron phthalocyanines.

İşci Ümit Ü Faponle Abayomi S AS Afanasiev Pavel P Albrieux Florian F Briois Valérie V Ahsen Vefa V Dumoulin Fabienne F Sorokin Alexander B AB de Visser Sam P SP

Chemical science 20150616 8

Iron(iv)-oxo species have been identified as the active intermediates in key enzymatic processes, and their catalytic properties are strongly affected by the equatorial and axial ligands bound to the metal, but details of these effects are still unresolved. In our aim to create better and more efficient oxidants of H-atom abstraction reactions, we have investigated a unique heteroleptic diiron phthalocyanine complex. We propose a novel intramolecular approach to determine the structural features ...[more]

PMID: 30155008

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Project description:Non-heme iron based halogenase enzymes promote selective halogenation of the sp3-C-H bond through iron(iv)-oxo-halide active species. During halogenation, competitive hydroxylation can be prevented completely in enzymatic systems. However, synthetic iron(iv)-oxo-halide intermediates often result in a mixture of halogenation and hydroxylation products. In this report, we have developed a new synthetic strategy by employing non-heme iron based complexes for selective sp3-C-H halogenation by overriding hydroxylation. A room temperature stable, iron(iv)-oxo complex, [Fe(2PyN2Q)(O)]2+ was directed for hydrogen atom abstraction (HAA) from aliphatic substrates and the iron(ii)-halide [FeII(2PyN2Q)(X)]+ (X, halogen) was exploited in conjunction to deliver the halogen atom to the ensuing carbon centered radical. Despite iron(iv)-oxo being an effective promoter of hydroxylation of aliphatic substrates, the perfect interplay of HAA and halogen atom transfer in this work leads to the halogenation product selectively by diverting the hydroxylation pathway. Experimental studies outline the mechanistic details of the iron(iv)-oxo mediated halogenation reactions. A kinetic isotope study between PhCH3 and C6D5CD3 showed a value of 13.5 that supports the initial HAA step as the RDS during halogenation. Successful implementation of this new strategy led to the establishment of a functional mimic of non-heme halogenase enzymes with an excellent selectivity for halogenation over hydroxylation. Detailed theoretical studies based on density functional methods reveal how the small difference in the ligand design leads to a large difference in the electronic structure of the [Fe(2PyN2Q)(O)]2+ species. Both experimental and computational studies suggest that the halide rebound process of the cage escaped radical with iron(iii)-halide is energetically favorable compared to iron(iii)-hydroxide and it brings in selective formation of halogenation products over hydroxylation.

Dataset Information

Site-selective formation of an iron(iv)-oxo species at the more electron-rich iron atom of heteroleptic ?-nitrido diiron phthalocyanines.

Publications

Site-selective formation of an iron(iv)-oxo species at the more electron-rich iron atom of heteroleptic μ-nitrido diiron phthalocyanines.

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