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Enhanced Rates of C-H Bond Cleavage by a Hydrogen-Bonded Synthetic Heme High-Valent Iron(IV) Oxo Complex.

ABSTRACT: Secondary coordination sphere interactions are critical in facilitating the formation, stabilization, and enhanced reactivity of high-valent oxidants required for essential biochemical processes. Herein, we compare the C-H bond oxidizing capabilities of spectroscopically characterized synthetic heme iron(IV) oxo complexes, F8Cmpd-II (F8 = tetrakis(2,6-difluorophenyl)porphyrinate), and a 2,6-lutidinium triflate (LutH+) Lewis acid adduct involving ferryl O-atom hydrogen-bonding, F8Cmpd-II(LutH+). Second-order rate constants utilizing C-H and C-D substrates were obtained by UV-vis spectroscopic monitoring, while products were characterized and quantified by EPR spectroscopy and gas chromatography (GC). With xanthene, F8Cmpd-II(LutH+) reacts 40 times faster (k2 = 14.2 M-1 s-1; -90 °C) than does F8Cmpd-II, giving bixanthene plus xanthone and the heme product [F8FeIIIOH2]+. For substrates with greater C-H bond dissociation energies (BDEs) F8Cmpd-II(LutH+) reacts with the second order rate constants k2(9,10-dihydroanthracene; DHA) = 0.485 M-1 s-1 and k2(fluorene) = 0.102 M-1 s-1 (-90 °C); by contrast, F8Cmpd-II is unreactive toward these substrates. For xanthene vs xanthene-(d2), large, nonclassical deuterium kinetic isotope effects are roughly estimated for both F8Cmpd-II and F8Cmpd-II(LutH+). The deuterated H-bonded analog, F8Cmpd-II(LutD+), was also prepared; for the reaction with DHA, an inverse KIE (compared to F8Cmpd-II(LutH+)) was observed. This work originates/inaugurates experimental investigation of the reactivity of authentic H-bonded heme-based FeIV?O compounds, critically establishing the importance of oxo H-bonding (or protonation) in heme complexes and enzyme active sites.

SUBMITTER: Ehudin MA

PROVIDER: S-EPMC6734939 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature

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Enhanced Rates of C-H Bond Cleavage by a Hydrogen-Bonded Synthetic Heme High-Valent Iron(IV) Oxo Complex.

Ehudin Melanie A MA Quist David A DA Karlin Kenneth D KD

Journal of the American Chemical Society 20190802 32

Secondary coordination sphere interactions are critical in facilitating the formation, stabilization, and enhanced reactivity of high-valent oxidants required for essential biochemical processes. Herein, we compare the C-H bond oxidizing capabilities of spectroscopically characterized synthetic heme iron(IV) oxo complexes, F8Cmpd-II (F8 = tetrakis(2,6-difluorophenyl)porphyrinate), and a 2,6-lutidinium triflate (LutH+) Lewis acid adduct involving ferryl O-atom hyd ...[more]

PMID: 31318198

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Project description:The thermodynamic properties of structurally similar Mn(III) and Mn(IV) complexes have been reinvestigated to understand their reactivity with substrates having C-H bonds. The complexes have the general formula [MnH(3)buea(O)](n-), where [H(3)buea](3-) is the tripodal ligand, tris[(N'-tert-butylureaylato)-N-ethylene]aminato. These complexes are unique because of the intramolecular hydrogen-bonding (H-bond) network surrounding the Mn-oxo units. The redox potentials for the Mn(III/IV)(O) couple was incorrectly assigned in earlier reports: the corrected value is -1.0 V vs Cp(2)Fe(+)/Cp(2)Fe in DMSO, while the Mn(IV/V)(O) process is -0.076 under the same conditions. The oxo ligand in the Mn(III)(O) complexes is basic with a pK(a) of 28.3; the basicity of the terminal oxo ligand in the Mn(IV)(O) complex is estimated to be approximately 15. These values were used to re-evalulate the O-H bond dissociation energy (BDE(OH)) of the corresponding Mn(II/III)-OH complexes: BDE(OH) values of 89 and 77 kcal/mol were determined for [Mn(III)H(3)buea(OH)](-) and [Mn(II)H(3)buea(OH)](2-), respectively. Both Mn(O) complexes react with 9,10-dihydroanthracene (DHA) to produce anthracene in nearly quantitative yields. This is surprising based on the low redox potiental of the complexes, suggesting the basicity of the oxo ligand is a major contributor to the observed reactivity. In contrast to the thermodynamic results, a comparative kinetic investigation found that the Mn(III)(O) complex reacts nearly 20 times faster than the Mn(IV)(O) complex. Activation parameters, determined from an Eyring analysis, found that the entropy of activation is significantly different between the two systems (DeltaDeltaS(++) = -35 eu, where DeltaDeltaS(++) = DeltaS(++)(Mn(IV)(O)) - DeltaS(++)(Mn(III)(O)). This unusual kinetic behavior can be explained in the context of the basicity of the oxo ligands that leads to different mechanisms: for [Mn(III)H(3)buea(O)](2-) a proton transfer-electron transfer mechanism is proposed, whereas for [Mn(IV)H(3)buea(O)](-) a hydrogen-atom transfer pathway is likely.

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

Enhanced Rates of C-H Bond Cleavage by a Hydrogen-Bonded Synthetic Heme High-Valent Iron(IV) Oxo Complex.

Publications

Enhanced Rates of C-H Bond Cleavage by a Hydrogen-Bonded Synthetic Heme High-Valent Iron(IV) Oxo Complex.

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