Dehalogenation Of Halophenols Research Articles

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.

K3MB5O10 (M = Zn and Cd) with d10 configuration: Efficient and reusable catalysts for dehalogenation of halophenols

Two isostructural d10 configuration non-centrosymmetric materials: K3ZnB5O10 (KZBO) and K3CdB5O10 (KCBO) can act as efficient and reusable catalysts in the dehalogenation of halophenols. More than 90% of the 2, 4-DXP were degraded within 10min with the dehalogenation efficiency 2, 4-DBP>2, 4-DCP>2, 4-DFP, the dehalogenation efficiency is almost 10 times higher than that of commercial P25 TiO2 catalyst in the present reaction conditions. The internal electric field due to the distorted [MO4] tetrahedral and [BO3] units promote the charge separation in the initial process of photoexcitation and d10 configuration of Zn and Cd with large dispersion is useful for photoexcited electron transfers without recombination, thus enhance the photocatalytic activity. The dehalogenation pathways with KCBO outlined both oxidative and reductive dehalogenation. Our work is expected to offer new insight into photocatalytic theory for better understandings to photocatalytic reactions and rational design and synthesis of photocatalysts with high activity.

Functional Switching of Amphitrite ornata Dehaloperoxidase from O2-Binding Globin to Peroxidase Enzyme Facilitated by Halophenol Substrate and H2O2

Amphitrite ornata dehaloperoxidase (DHP) is the first heme-containing globin possessing a native peroxidase enzymatic activity. DHP catalyzes the H(2)O(2)-dependent dehalogenation of halophenols. By possessing this detoxifying enzymatic activity, these organisms are able to thrive in an environment contaminated with toxic haloaromatics. It has been proposed that DHP evolved from a dioxygen carrier globin protein and therefore possesses dual physiological roles of O(2) carrier and dehaloperoxidase. Although DHP is isolated in the catalytically inactive oxyferrous state (oxy-DHP), we find that the combination of H(2)O(2) and the substrate 2,4,6-trichlorophenol (TCP) brings about facile switching of oxy-DHP to the enzymatically active ferric state via a process likely involving substrate radicals (TCP*). In contrast, in the absence of TCP, H(2)O(2) alone converts oxy-DHP to an inactive state (compound RH) instead of oxidizing the enzyme to the ferric state. Further, although the rate of autoxidation of oxy-DHP is somewhat enhanced by the presence of TCP, the effect is too small to be the functional switch. Instead, both substrate and H(2)O(2) are needed to convert oxy-DHP to the catalytically active ferric state. These observations provide a physiological link between the O(2) carrier role of the ferrous protein and the peroxidase activity of the ferric enzyme in this bifunctional protein.

Spectroscopic Study of Substrate Binding to the Carbonmonoxy Form of Dehaloperoxidase fromAmphitriteornata

Dehaloperoxidase (DHP) is a globular heme enzyme found in the marine worm Amphitrite ornata that can catalyze the dehalogenation of halophenols to the corresponding quinones by using hydrogen peroxide as a cosubstrate. Its three-dimensional fold is surprisingly similar to that of the oxygen storage protein myoglobin (Mb). A key structural feature common to both DHP and Mb is the existence of multiple conformations of the distal histidine. In DHP, the conformational flexibility may be involved in promotion of substrate and cosubstrate entry and exit. Here we have explored the dynamics of substrate binding in DHP using Fourier transform infrared spectroscopy and flash photolysis. A number of discrete conformations at the active site were identified from the appearance of multiple CO absorbance bands in the infrared region of the spectrum. Upon photolysis at cryogenic temperatures, the CO molecules are trapped at docking sites within the protein matrix, as inferred from the appearance of several photoproduct bands characteristic of each site. Substrate binding stabilizes the protein by approximately 20 kJ/mol. The low yield of substrate-bound DHP at ambient temperature points toward a steric inhibition of substrate binding by carbon monoxide.

Spectroscopic characterization of the ferric states of Amphitrite ornata dehaloperoxidase and Notomastus lobatus chloroperoxidase: His-ligated peroxidases with globin-like proximal and distal properties

Amphitrite ornata dehaloperoxidase (DHP) and Notomastus lobatus chloroperoxidase (NCPO) catalyze the peroxide-dependent dehalogenation of halophenols and halogenation of phenols, respectively. Both enzymes have histidine (His) as their proximal heme iron ligand. Crystallographic examination of DHP revealed that it has a globin fold [M.W. LaCount, E. Zhang, Y.-P. Chen, K. Han, M.M. Whitton, D.E. Lincoln, S.A. Woodin, L. Lebioda, J. Biol. Chem. 275 (2000) 18712–18716] and kinetics studies established that ferric DHP is the active state [R.L. Osborne, L.O. Taylor, K. Han, B. Ely, J.H. Dawson, Biochem. Biophys. Res. Commun. 324 (2004) 1194–1198]. NCPO likely has these same properties. Previous work with His-ligated heme proteins has revealed characteristic spectral distinctions between dioxygen binding globins and peroxide-activating peroxidases. Since DHP, and likely NCPO, is a peroxide-activating globin, we have sought to determine in the present investigation whether the ferric resting states of these two novel heme-containing enzymes are myoglobin-like or peroxidase-like. To do so, we have examined their exogenous ligand-free ferric states as well as their azide, imidazole and NO bound ferric adducts (and ferrous–NO complexes) with UV–Visible absorption and magnetic circular dichroism spectroscopy. We have also compared each derivative to the analogous states of horse heart myoglobin (Mb) and horseradish peroxidase (HRP). The spectra observed for parallel forms of DHP and NCPO are virtually identical to each other as well as to the spectra of the same Mb states, while being less similar to the spectra of corresponding HRP derivatives. From these data, we conclude that exogenous ligand-free ferric DHP and NCPO are six-coordinate with water and neutral His as ligands. This coordination structure is distinctly different from the ferric resting state of His-ligated peroxidases and indicates that DHP and NCPO do not activate bound peroxide through a mechanism dependent on a push effect imparted by a partially ionized proximal His as proposed for typical heme peroxidases.

C. fumagoChloroperoxidase is also a Dehaloperoxidase: Oxidative Dehalogenation of Halophenols

We have examined the H2O2-dependent oxidative dehalogenation of 2,4,6-trihalophenols and p-halophenols catalyzed by Caldariomyces fumago chloroperoxidase (CCPO). CCPO is significantly more robust than other peroxidases and can function under harsher reaction conditions, and so its ability to dehalogenate halophenols could lead to its use as a bioremediation catalyst for aromatic dehalogenation reactions. Optimal catalysis occurred under acidic conditions (100 mM potassium phosphate solution, pH 3.0). UV-visible absorption spectroscopy, high-performance liquid chromatography, and gas chromatography/mass spectrometry clearly identified the oxidized reaction product for CCPO-catalyzed dehalogenation of 2,4,6-trihalophenols as the corresponding 2,6-dihalo-1,4-benzoquinones. This reaction has previously been reported for two His-ligated heme-containing peroxidases (see Osborne, R. L.; Taylor, L. O.; Han, K. P.; Ely, B.; Dawson, J. H. Biochem. Biophys. Res. Commun. 2004, 324, 1194-1198), but this is the first example of a Cys-ligated heme-containing peroxidase functioning as a dehaloperoxidase. The relative catalytic efficiency (turnover number) of CCPO reported herein is comparable to that of horseradish peroxidase (Ferrari, R. P.; Laurenti, E.; Trotta, F. J. Biol. Inorg. Chem. 1965, 4, 232-237). The mechanism of dehalogenation has been probed using p-halophenols as substrates. Here the major product is a dimer with 1,4-benzoquinone as the minor product. An electron-transfer mechanism is proposed that accounts for the products formed from both the 2,4,6-trihalo- and p-halophenols. Finally, we note that this is the first case of a peroxidase known primarily for its halogenation ability being shown to also dehalogenate substrates.

Reductive Dehalogenation of Halophenols in Sulfite—Bisulfate Medium.

AbstractFor Abstract see ChemInform Abstract in Full Text.

Reductive dehalogenation of halophenols in sulfite–bisulfate medium

The KHSO 4–Na 2SO 3 system is found to be simple and inexpensive for reductive elimination of halogens (Br, I) from the corresponding halophenols under reflux conditions in dry methanol. Under similar conditions the reaction is sluggish with chlorophenols.

Highly efficient dehalogenation using hydroxyapatite-supported palladium nanocluster catalyst with molecular hydrogen

A hydroxyapatite-supported Pd nanocluster (PdHAP) efficiently catalysed the dehalogenation of various organic halides in the presence of atmospheric molecular hydrogen; chlorobenzene gave benzene in an excellent TON of 10000 for 10 h. Moreover, the dehalogenation of halophenols in aqueous conditions was also achieved.

A Novel Application of Hβ‐Zeolite in Catalytic Dehalogenation of Halophenols.

A new application of Hβ-zeolite for debromination of bromophenols and deiodination of iodophenols is presented in this note. The heterogeneous catalyst can be recovered and recycled effectively for subsequent reactions. The catalyst was found ineffective for similar action on chlorophenols.

A novel application of Hβ-zeolite in catalytic dehalogenation of halophenols

A new application of Hβ-zeolite for debromination of bromophenols and deiodination of iodophenols is presented in this note. The heterogeneous catalyst can be recovered and recycled effectively for subsequent reactions. The catalyst was found ineffective for similar action on chlorophenols.

The Unusual Reactivities ofAmphitrite ornataDehaloperoxidase andNotomastus lobatusChloroperoxidase Do Not Arise from a Histidine Imidazolate Proximal Heme Iron Ligand

Notomastus lobatus chloroperoxidase (NCPO) and Amphitrite ornata dehaloperoxidase (DHP) catalyze the halogenation of phenols and dehalogenation of halophenols, respectively. Both enzymes require peroxide for activity and have recently been shown to contain histidine (His) as their proximal heme iron ligand. DHP is the only heme enzyme known to catalyze peroxide-dependent defluorination reactions, and NCPO is the first His-ligated heme-containing peroxidase capable of chlorinating halogen acceptors using chloride as the halogen donor. To probe the roles of the proximal His ligands in the mechanism of action of these two novel peroxidases, they have been examined by resonance Raman and infrared spectroscopy to determine the vibrational properties of their deoxyferrous and ferrous−CO derivatives. Previous studies of His-ligated heme proteins have revealed characteristic distinctions between dioxygen-binding globins and peroxidases. In the latter, the spectral properties are indicative of strong hydrogen bond...