Defluorination of Fluorophenols by a Nonheme Iron(IV)-Oxo Species: Observation of a New Intermediate Along the Reaction.

High-valent iron(IV)-oxo intermediates are versatile oxidants in the biotransformation of various substrates by metalloenzymes and catalyze essential reactions for human health as well as in the biodegradation of toxic organic pollutants in the environment. Herein, we report a biomimetic system that efficiently reacts with halophenols through defluorination reactions and characterize various short-lived intermediates along the reaction mechanism. We study the reactivity pattern of a nonheme iron(IV)-oxo species with a series of trihalophenols (X=F, Cl, Br). A combined experimental and computational study reveals that the oxidative dehalogenation of 2,4,6-trifluorophenol is initiated with an H-atom abstraction from the phenolic group by the iron(IV)-oxo species resulting in the formation of a phenolate radical and an iron(III)-hydroxo species. This iron(III)-hydroxo species forms an adduct with the oxidized substrate with λmax at 558 nm which subsequently decays to give quinones as products.

Oxidative dehalogenation of halophenols by high-valent nonheme iron(IV)-oxo intermediates.

Mononuclear high-valent iron(IV)-oxo intermediates are excellent oxidants towards oxygenation reactions by heme and nonheme metalloenzymes and their model systems. One of the most important functions of these intermediates in nature is to detoxify various environmental pollutants. Organic substrates, such as halogenated phenols, are known to be water pollutants which can be degraded to their less hazardous forms through an oxidation reaction by iron(IV)-oxo complexes. Metalloproteins in nature utilize various types of second-coordination sphere interactions to anchor the substrate in the vicinity of the active site. This concept of substrate-binding is well-known for natural enzymes, but is elusive for the relevant biomimetic model systems. Herein, we report the oxidative reactivity patterns of an iron(IV)-oxo intermediate, [FeIV(O)(2PyN2Q)]2+, (2PyN2Q = 1,1-di(pyridin-2yl)-N,N-bis(quinolin-2-ylmethyl)methanamine) with a series of mono-, di- and tri-halophenols. A detailed experimental study shows that the dehalogenation reactions of the halophenols by such iron(IV)-oxo intermediates proceed via an initial hydrogen atom abstraction from the phenolic O-H group. Furthermore, based on the size and nucleophilicity of the halophenol, an intermediate substrate-bound species forms that is a phenolate adduct to the ferric species, which thereafter leads to the formation of the corresponding products.

A comprehensive insight into aldehyde deformylation: mechanistic implications from biology and chemistry.

Aldehyde deformylation is an important reaction in biology, organic chemistry and inorganic chemistry and the process has been widely applied and utilized. For instance, in biology, the aldehyde deformylation reaction has wide differences in biological function, whereby cyanobacteria convert aldehydes into alkanes or alkenes, which are used as natural products for, e.g., defense mechanisms. By contrast, the cytochromes P450 catalyse the biosynthesis of hormones, such as estrogen, through an aldehyde deformylation reaction step. In organic chemistry, the aldehyde deformylation reaction is a common process for replacing functional groups on a molecule, and as such, many different synthetic methods and procedures have been reported that involve an aldehyde deformylation step. In bioinorganic chemistry, a variety of metal(iii)-peroxo complexes have been synthesized as biomimetic models and shown to react efficiently with aldehydes through deformylation reactions. This review paper provides an overview of the various aldehyde deformylation reactions in organic chemistry, biology and biomimetic model systems, and shows a broad range of different chemical reaction mechanisms for this process. Although a nucleophilic attack at the carbonyl centre is the consensus reaction mechanism, several examples of an alternative electrophilic reaction mechanism starting with hydrogen atom abstraction have been reported as well. There is still much to learn and to discover on aldehyde deformylation reactions, as deciphered in this review paper.

Sluggish reactivity by a nonheme iron(iv)-tosylimido complex as compared to its oxo analogue.

High-valent iron-nitrido intermediates have been postulated as reactive intermediates in various enzymes, including the nitrogenases and the cytochromes P450, but so far few have been trapped and characterized. As little is known about their oxidative and spectroscopic properties, we decided to create biomimetic models of iron(iv)-imido complexes and compare their structure and reactivity with analogous iron(iv)-oxo systems. In this work we report the synthesis and spectroscopic characterization of a novel [FeIV(NTs)(Bntpen)]2+ complex (Bntpen = N1-benzyl-N1,N2,N2-tris(pyridine-2-ylmethyl)ethane-1,2-diamine) and study its reactivity patterns with respect to hydrogen atom abstraction and nitrogen atom transfer reactions. The work is compared with analogous pentadentate ligand systems as well as with iron(iv)-oxo species with the same ligand features and highlights the differences in chemical properties and reactivity patterns. It is shown that the reactivity is dependent on the metal ligand system that affects the physicochemical properties of the oxidant such as the redox potential, which is the main driving force for the reaction mechanism with substrates.

Hydrogen by Deuterium Substitution in an Aldehyde Tunes the Regioselectivity by a Nonheme Manganese(III)-Peroxo Complex.

Mononuclear nonheme MnIII -peroxo complexes are important intermediates in biology, and take part in oxygen activation by photosystem II. Herein, we present work on two isomeric biomimetic side-on MnIII -peroxo intermediates with bispidine ligand system and reactivity patterns with aldehydes. The complexes are characterized with UV/Vis and mass spectrometric techniques and reaction rates with cyclohexane carboxaldehyde (CCA) are measured. The reaction gives an unusual regioselectivity switch from aliphatic to aldehyde hydrogen atom abstraction upon deuteration of the substrate, leading to the corresponding carboxylic acid product for the latter, while the former gives a deformylation reaction. Mechanistic details are established from kinetic isotope effect studies and density functional theory calculations. Thus, replacement of C-H by C-D raises the hydrogen atom abstraction barriers and enables a regioselectivity switch to a competitive pathway that is slightly higher in energy.