Oxidative dehalogenation of trichlorophenol catalyzed by a promiscuous artificial heme-enzyme

Sekretareva, Alina; D’Alonzo, Daniele; Leone, Linda; Pavone, Vincenzo; Lombardi, Angela; Nastri, Flavia

doi:10.1039/d2ra00811d

Cited by 13 publications

(18 citation statements)

References 58 publications

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“…Indeed, the TON value that referred to the Fe-MC6*a-catalyzed conversion of 4-CP was 325 (entry 3), whereas the reaction with 2,4-dichlorophenol (2,4-DCP) proceeded with a TON value of 2588 (entry 6). As already reported [38], in the case of 2,4,6-trichlorophenol (2,4,6-TCP), the TON value further increased up to 3850 (entry 8). Similarly, the TON that referred to the reaction of 2,4,6-trifluorophenol (2,4,6-TFP) was 3825 (entry 7).…”

Section: H 2 O 2 -Dependent Dehalogenation Activity Of Fe(iii)-mc6*asupporting

confidence: 77%

“…The iron-containing derivative, Fe-MC6*a, mainly acts as a peroxidase model, with intriguing catalytic properties in the oxidation of various substrates [36,37]. When assayed in the dehalogenation reaction of the pollutant 2,4,6-trichlorophenol (TCP), Fe-MC6*a exhibited the highest catalytic efficiency among both natural and artificial metalloenzymes, tested in the same reaction [38] (Figure 1c).…”

Section: Introductionmentioning

confidence: 99%

“…The excellent behavior of Fe-MC6*a in TCP dehalogenation [38] encouraged us to carry out a more extensive evaluation of its reactivity toward a variety of other halogenated phenols, including mono-, di-, tri-and penta-halophenols (Figure 1d). Halophenols represent interesting substrates for oxidative catalysis.…”

Section: Introductionmentioning

confidence: 99%

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Selective Oxidation of Halophenols Catalyzed by an Artificial Miniaturized Peroxidase

D’Alonzo

Fenza

Pavone

et al. 2023

IJMS

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The development of artificial enzymes for application in sustainable technologies, such as the transformation of environmental pollutants or biomass, is one of the most challenging goals in metalloenzyme design. In this work, we describe the oxidation of mono-, di-, tri- and penta-halogenated phenols catalyzed by the artificial metalloenzyme Fe-MC6*a. It promoted the dehalogenation of 4-fluorophenol into the corresponding 1,4-benzoquinone, while under the same experimental conditions, 4-chloro, 4-bromo and 4-iodophenol were selectively converted into higher molecular weight compounds. Analysis of the 4-chlorophenol oxidation products clarified that oligomers based on C-O bonds were exclusively formed in this case. All results show that Fe-MC6*a holds intriguing enzymatic properties, as it catalyzes halophenol oxidation with substrate-dependent chemoselectivity.

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Section: H 2 O 2 -Dependent Dehalogenation Activity Of Fe(iii)-mc6*asupporting

confidence: 77%

Section: Introductionmentioning

confidence: 99%

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Selective Oxidation of Halophenols Catalyzed by an Artificial Miniaturized Peroxidase

D’Alonzo

Fenza

Pavone

et al. 2023

IJMS

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“…As described above, FeMC6*a is a promiscuous, artificial miniaturized peroxidase. [44,50] The reduced size of this catalyst compared to natural peroxidases, coupled with the easy scaleup of its synthetic route, offers significant advantages for a variety of practical applications. [49,52] To evaluate its potential as a substitute for natural enzymes in LFiA technology, its catalytic activity toward the H 2 O 2 -mediated TMB oxidation was assayed.…”

Section: Evaluation Of Femc6*a Stability/activity Under Operational C...mentioning

confidence: 99%

“…[44] Despite its simplified structure, experimental data have proven the ability of FeMC6*a to outperform natural and artificial biocatalysts in catalyzing several oxidation reactions. [49,50] The success of this approach has paved the way to further widen the functional repertoire of FeMC6*a, exploring its catalytic potential after conjugation on gold electrodes and nanomaterials. [51,52] Since FeMC6*a retains its structure and catalytic behavior when conjugated to gold nanomaterials, the size of this mini-enzyme (radius of gyration ≈ 1 nm, compared to HRP ≈ 3 nm) [53] grants the possibility of drastically influencing the specific activity of functionalized nanomaterials, by increasing the active-site density.…”

Section: Introductionmentioning

confidence: 99%

An Artificial Miniaturized Peroxidase for Signal Amplification in Lateral Flow Immunoassays

Renzi

Piper

Nastri

et al. 2023

Small

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Signal amplification strategies are widely used for improving the sensitivity of lateral flow immunoassays (LFiAs). Herein, the artificial miniaturized peroxidase Fe(III)‐MimochromeVI*a (FeMC6*a), immobilized on gold nanoparticles (AuNPs), is used as a strategy to obtain catalytic signal amplification in sandwich immunoassays on lateral flow strips. The assay scheme uses AuNPs decorated with the mini‐peroxidase FeMC6*a and anti‐human‐IgG as a detection antibody (dAb), for the detection of human‐IgG, as a model analyte. Recognition of the analyte by the capture and detection antibodies is first evidenced by the appearance of a red color in the test line (TL), due to the accumulation of AuNPs. Subsequent addition of 3,3′,5,5′‐tetramethylbenzidine (TMB) induces an increase of the test line color, due to the TMB being converted into an insoluble colored product, catalyzed by FeMC6*a. This work shows that FeMC6*a acts as an efficient catalyst in paper, increasing the sensitivity of an LFiA up to four times with respect to a conventional LFiA. Furthermore, FeMC6*a achieves lower limits of detection that are found in control experiments where it is replaced with horseradish peroxidase (HRP), its natural counterpart. This study represents a significant proof‐of‐concept for the development of more sensitive LFiAs, for different analytes, based on properly designed artificial metalloenzymes.

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Peptides and metal ions: A successful marriage for developing artificial metalloproteins

Leone,

De Fenza,

Esposito

et al. 2024

Journal of Peptide Science

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The mutual relationship between peptides and metal ions enables metalloproteins to have crucial roles in biological systems, including structural, sensing, electron transport, and catalytic functions. The effort to reproduce or/and enhance these roles, or even to create unprecedented functions, is the focus of protein design, the first step toward the comprehension of the complex machinery of nature. Nowadays, protein design allows the building of sophisticated scaffolds, with novel functions and exceptional stability. Recent progress in metalloprotein design has led to the building of peptides/proteins capable of orchestrating the desired functions of different metal cofactors. The structural diversity of peptides allows proper selection of first‐ and second‐shell ligands, as well as long‐range electrostatic and hydrophobic interactions, which represent precious tools for tuning metal properties. The scope of this review is to discuss the construction of metal sites in de novo designed and miniaturized scaffolds. Selected examples of mono‐, di‐, and multi‐nuclear binding sites, from the last 20 years will be described in an effort to highlight key artificial models of catalytic or electron‐transfer metalloproteins. The authors' goal is to make readers feel like guests at the marriage between peptides and metal ions while offering sources of inspiration for future architects of innovative, artificial metalloproteins.

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Oxidative dehalogenation of trichlorophenol catalyzed by a promiscuous artificial heme-enzyme

Abstract: The artificial metalloenzyme FeMC6*a is able to perform the H2O2-mediated dechlorination of 2,4,6-trichlorophenol with unrivalled catalytic efficiency, highlighting its potential application for the removal of toxic pollutants.

Cited by 13 publications

References 58 publications

Selective Oxidation of Halophenols Catalyzed by an Artificial Miniaturized Peroxidase

Selective Oxidation of Halophenols Catalyzed by an Artificial Miniaturized Peroxidase

An Artificial Miniaturized Peroxidase for Signal Amplification in Lateral Flow Immunoassays

Peptides and metal ions: A successful marriage for developing artificial metalloproteins

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