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Influence of the distal guanidine group on the rate and selectivity of O2 reduction by iron porphyrin.

ABSTRACT: The O2 reduction reaction (ORR) catalysed by iron porphyrins with covalently attached pendant guanidine groups is reported. The results show a clear enhancement in the rate and selectivity for the 4e-/4H+ ORR. In situ resonance Raman investigations show that the rate determining step (rds) is O2 binding to ferrous porphyrins in contrast to the case of mononuclear iron porphyrins and heme/Cu analogues where the O-O bond cleavage of a heme peroxide is the rds. The selectivity is further enhanced when an axial imidazole ligand is introduced. Thus, the combination of the axial imidazole ligand and pendant guanidine ligand, analogous to the active site of peroxidases, is determined to be very effective in enabling a facile and selective 4e-/4H+ ORR.

SUBMITTER: Ghatak A

PROVIDER: S-EPMC6993607 | biostudies-literature | 2019 Nov

REPOSITORIES: biostudies-literature

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Influence of the distal guanidine group on the rate and selectivity of O2 reduction by iron porphyrin.

Ghatak Arnab A Bhakta Snehadri S Bhunia Sarmistha S Dey Abhishek A

Chemical science 20190829 42

The O2 reduction reaction (ORR) catalysed by iron porphyrins with covalently attached pendant guanidine groups is reported. The results show a clear enhancement in the rate and selectivity for the 4e-/4H+ ORR. In situ resonance Raman investigations show that the rate determining step (rds) is O2 binding to ferrous porphyrins in contrast to the case of mononuclear iron porphyrins and heme/Cu analogues where the O-O bond cleavage of a heme peroxid ...[more]

PMID: 32055338

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Project description:Cytochrome P450 enzymes are heme based monoxygenases that catalyse a range of oxygen atom transfer reactions with various substrates, including aliphatic and aromatic hydroxylation as well as epoxidation reactions. The active species is short-lived and difficult to trap and characterize experimentally, moreover, it reacts in a regioselective manner with substrates leading to aliphatic hydroxylation and epoxidation products, but the origin of this regioselectivity is poorly understood. We have synthesized a model complex and studied it with low-pressure Fourier transform-ion cyclotron resonance (FT-ICR) mass spectrometry (MS). A novel approach was devised using the reaction of [FeIII(TPFPP)]+ (TPFPP = meso-tetrakis(pentafluorophenyl)porphinato dianion) with iodosylbenzene as a terminal oxidant which leads to the production of ions corresponding to [FeIV(O)(TPFPP+?)]+. This species was isolated in the gas-phase and studied in its reactivity with a variety of olefins. Product patterns and rate constants under Ideal Gas conditions were determined by FT-ICR MS. All substrates react with [FeIV(O)(TPFPP+?)]+ by a more or less efficient oxygen atom transfer process. In addition, substrates with low ionization energies react by a charge-transfer channel, which enabled us to determine the electron affinity of [FeIV(O)(TPFPP+?)]+ for the first time. Interestingly, no hydrogen atom abstraction pathways are observed for the reaction of [FeIV(O)(TPFPP+?)]+ with prototypical olefins such as propene, cyclohexene and cyclohexadiene and also no kinetic isotope effect in the reaction rate is found, which suggests that the competition between epoxidation and hydroxylation - in the gas-phase - is in favour of substrate epoxidation. This notion further implies that P450 enzymes will need to adapt their substrate binding pocket, in order to enable favourable aliphatic hydroxylation over double bond epoxidation pathways. The MS studies yield a large test-set of experimental reaction rates of iron(iv)-oxo porphyrin cation radical complexes, so far unprecedented in the gas-phase, providing a benchmark for calibration studies using computational techniques. Preliminary computational results presented here confirm the observed trends excellently and rationalize the reactivities within the framework of thermochemical considerations and valence bond schemes.

Dataset Information

Influence of the distal guanidine group on the rate and selectivity of O2 reduction by iron porphyrin.

Publications

Influence of the distal guanidine group on the rate and selectivity of O<sub>2</sub> reduction by iron porphyrin.

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