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Analytical Chemistry May 2023The peroxidase (POD)-like nanozyme typically requires the addition of exogenous HO. To address the limitation, previous work mainly adopted a cascade strategy for HO...
The peroxidase (POD)-like nanozyme typically requires the addition of exogenous HO. To address the limitation, previous work mainly adopted a cascade strategy for HO production. Herein, we propose a new light-driven self-cascade strategy to construct POD-like nanozymes without exogenous HO. The model nanozyme resorcinol-formaldehyde resin-Fe (RF-Fe) is synthesized with the hydroxyl-rich photocatalytic material RF as the carrier to in situ chelate metal oxides, which can simultaneously achieve the functions of in situ HO generation under irradiation and substrate oxidation via POD-like behavior. Notably, RF-Fe exhibits high affinity to HO, attributed to the excellent adsorption ability and hydroxyl-rich feature of RF. Furthermore, the dual photoelectrode-assisted photofuel cell was further constructed with a high-power density of 120 ± 5 μW cm based on the RF-Fe photocathode. This work not only demonstrates the new self-cascade strategy of in situ generation of catalysis substrates but also provides an opportunity to extend the catalytical field.
Topics: Peroxidase; Hydrogen Peroxide; Peroxidases; Adsorption; Catalysis; Coloring Agents; Hydroxyl Radical
PubMed: 37072890
DOI: 10.1021/acs.analchem.3c00627 -
Analytical Chemistry Mar 2022Metal-organic frameworks (MOFs) are widely used to mimic enzymes for catalyzing chemical reactions; however, low enzyme activity limit their large-scale application. In...
Metal-organic frameworks (MOFs) are widely used to mimic enzymes for catalyzing chemical reactions; however, low enzyme activity limit their large-scale application. In this work, gold nanorods/metal-organic frameworks (Au NRs/Fe-MOF) hybrids were successfully synthesized for photo-enhanced peroxidase-like catalysis and surface-enhanced Raman spectroscopy (SERS). The enzyme-like activity of Au NRs/Fe-MOF hybrids was significantly enhanced under localized surface plasmon resonance (LSPR), because the hot electrons produced on Au NRs surface were transferred into Fe-MOF, activating the Fenton reaction by Fe/Fe conversion and preventing the recombination of hot electrons and holes. This photo-enhanced enzyme-like catalytic performance was investigated by X-ray photoelectron spectrometry (XPS), electrochemical analysis, activation energy measurement, and in situ Raman spectroscopy. Afterward, Methylene Blue (MB) was chosen to demonstrate the photo-enhanced peroxidase-like performance of Au NRs/Fe-MOFs. The Au NRs/Fe-MOF caused chemical and electromagnetic enhancement of Raman signals and exhibited a great potential for the detection of toxic chemicals and biological molecules. The detection limit of MB concentration is 9.3 × 10 M. In addition, the Au NRs/Fe-MOF hybrids also showed excellent stability and reproducibility for photo-enhanced peroxidase-like catalysis. These results show that nanohybrids have great potential in many fields, such as sensing, cancer therapy, and energy harvesting.
Topics: Coloring Agents; Gold; Metal-Organic Frameworks; Methylene Blue; Nanotubes; Peroxidase; Peroxidases; Reproducibility of Results
PubMed: 35235310
DOI: 10.1021/acs.analchem.2c00036 -
Biochimica Et Biophysica Acta. Proteins... Jan 2020Human peroxidasin 1 is a multidomain peroxidase situated in the basement membrane. The iron enzyme with covalently bound heme oxidizes bromide to hypobromous acid which...
Human peroxidasin 1 is a multidomain peroxidase situated in the basement membrane. The iron enzyme with covalently bound heme oxidizes bromide to hypobromous acid which facilitates the formation of distinct sulfilimine cross-links in the collagen IV network and therefore contributes to its mechanical stability. Additional to the catalytically active peroxidase domain peroxidasin comprises a leucine rich repeat domain, four Ig domains and a C-terminal von Willebrand factor type C module (VWC). Peroxidasin has been shown to form homotrimers involving two redox-sensitive cysteine residues and to undergo posttranslational C-terminal proteolytic cleavage. The present study on several recombinantly produced truncated peroxidasin variants showed that the VWC is not required for trimer formation whereas the alpha-helical linker region located between the peroxidase domain and the VWC is crucial for trimerization. Our data furthermore implies that peroxidasin oligomerization occurs intracellularly before C-terminal cleavage. For the first time we present overall solution structures of monomeric and trimeric truncated peroxidasin variants which were determined by rotary shadowing combined with transmission electron microscopy and by small-angle X-ray scattering (SAXS). A triangular arrangement of the peroxidase domains to each other within the homotrimer was revealed and this structure was confirmed by a model of trimeric peroxidase domains. Our SAXS data showed that the Ig domains are highly flexible and interact with the peroxidase domain and that within the homotrimer each alpha-helical linker region interacts with the respective adjacent peroxidase domain. The implications of our findings on the structure-function relationship of peroxidasin are discussed.
Topics: Extracellular Matrix Proteins; Humans; Models, Molecular; Peroxidase; Protein Multimerization; Recombinant Proteins; Peroxidasin
PubMed: 31295557
DOI: 10.1016/j.bbapap.2019.07.002 -
Angewandte Chemie (International Ed. in... Jun 2022We present a facile route towards a dual single-atom nanozyme composed of Zn and Mo, which utilizes the non-covalent nano-assembly of polyoxometalates, supramolecular...
We present a facile route towards a dual single-atom nanozyme composed of Zn and Mo, which utilizes the non-covalent nano-assembly of polyoxometalates, supramolecular coordination complexes as the metal-atom precursor, and a macroscopic amphiphilic aerogel as the supporting substrate. The dual single-atoms of Zn and Mo have a high content (1.5 and 7.3 wt%, respectively) and exhibit a synergistic effect and a peroxidase-like activity. The Zn/Mo site was identified as the main active center by X-ray absorption fine structure spectroscopy and density functional theory calculation. The detection of versatile analytes, including intracellular H O , glucose in serum, cholesterol, and ascorbic acid in commercial beverages was achieved. The nanozyme has an outstanding stability and maintained its performance after one year's storage. This study develops a new peroxidase-like nanozyme and provides a robust synthetic strategy for single-atom catalysts by utilizing an aerogel as a facile substrate that is capable of stabilizing various metal atoms.
Topics: Antioxidants; Catalysis; Peroxidase; Peroxidases; Zinc
PubMed: 35238141
DOI: 10.1002/anie.202116170 -
Journal of Molecular Graphics &... Sep 2021Our earlier studies show that the peroxidase activity of cyclooxygenase 1 and 2 (COX-1 and COX-2) can be reactivated in vitro and in vivo by the presence of certain...
Our earlier studies show that the peroxidase activity of cyclooxygenase 1 and 2 (COX-1 and COX-2) can be reactivated in vitro and in vivo by the presence of certain naturally-occurring flavonoids such as quercetin and myricetin, which serve as reducing cosubstrates. These compounds can activate COX at nanomolar concentrations. In the present study, quercetin is used as a representative model compound to investigate the chemical mechanism by which the peroxidase activity of human COX-1 and COX-2 is reactivated after each catalytic cycle. Molecular docking and quantum mechanics calculations are carried out to probe the interactions of quercetin with the peroxidase sites of COX-1/2 and the reactivation mechanism. It is found that some of the partially-ionized states of quercetin can bind tightly and closely inside the peroxidase active sites of the COX enzymes and directly interact with heme Fe ion. While quercetin contains several phenolic hydroxyl groups, it is found that only the C-3'-OH group can effectively donate an electron for the reduction of heme because it not only can bind closely and tightly inside the peroxidase sites of COX-1/2, but it can also facilely donate an electron to heme Fe ion. This investigation provides a mechanistic explanation for the chemical process by which quercetin reactivates COX-1/2 peroxidases. This knowledge would aid in the rational design of drugs that can selectively target the peroxidase sites of COX-1/2 either as activators or inhibitors.
Topics: Cyclooxygenase 2; Humans; Molecular Docking Simulation; Peroxidase; Peroxidases; Quercetin
PubMed: 34091174
DOI: 10.1016/j.jmgm.2021.107941 -
Small (Weinheim An Der Bergstrasse,... Mar 2023Multi-nanozymes are widely applied in disease treatment, biosensing, and other fields. However, most current multi-nanozyme systems exhibit only moderate activity since...
Multi-nanozymes are widely applied in disease treatment, biosensing, and other fields. However, most current multi-nanozyme systems exhibit only moderate activity since reaction microenvironments of different nanozyme are often distinct or even incompatible. Conventional assemble strategies are inapplicable for designing multi-nanozymes consisting of incompatible nanozymes. Herein, a versatile fiber-based compartmentalization strategy is developed to construct multi-nanozyme system capable of simultaneously performing incompatible reactions. In this system, the incompatible nanozymes are spatially distributed in distinct compartmentalized fibers, where different microenvironments can be tailored by controlling the doping reagent, endowing each nanozymes with the preferential microenvironments to exhibit their highest activity. As a proof of concept, pH-incompatible peroxidase-like and catalase-like catalytic reactions are tested to verify the feasibility of this strategy. By doping with benzoic acid in the desired location, the two pH-incompatible nanozymes can work simultaneously without interference. Further, it is demonstrated that the oxygen supply and antimicrobial power of the integrated platform can be applied for accelerating diabetic wound healing. It is hoped that this work provides a way to integrate incompatible nanozyme and broadens the application potential of multi-nanozymes.
Topics: Peroxidases; Peroxidase; Wound Healing; Coloring Agents; Catalysis; Diabetes Mellitus
PubMed: 36541749
DOI: 10.1002/smll.202206707 -
Chemical Communications (Cambridge,... Jun 2023-Acetylated microperoxidase-11 and G-quadruplex DNA are shown to form a stable "peptide-hemin/DNA" hybrid-complex, in which the peroxidase activity at the interface...
-Acetylated microperoxidase-11 and G-quadruplex DNA are shown to form a stable "peptide-hemin/DNA" hybrid-complex, in which the peroxidase activity at the interface between hemin and the G-quartet planes exponentially increases with increasing value.
Topics: Hemin; DNA; Peroxidases; G-Quadruplexes; DNA, Catalytic; Peroxidase; Biosensing Techniques
PubMed: 37272293
DOI: 10.1039/d3cc00752a -
Molecules (Basel, Switzerland) Dec 2022Recent decades have witnessed the rapid progress of nanozymes and their high promising applications in catalysis and bioclinics. However, the comprehensive synthetic...
Recent decades have witnessed the rapid progress of nanozymes and their high promising applications in catalysis and bioclinics. However, the comprehensive synthetic procedures and harsh synthetic conditions represent significant challenges for nanozymes. In this study, monodisperse, ultrasmall gold clusters with peroxidase-like activity were prepared via a simple and robust one-pot method. The reaction of clusters with HO and 3,3',5,5'-tetramethylbenzidine (TMB) followed the Michaelis-Menton kinetics. In addition, in vitro experiments showed that the prepared clusters had good biocompatibility and cell imaging ability, indicating their future potential as multi-functional materials.
Topics: Peroxidase; Gold; Hydrogen Peroxide; Peroxidases; Catalysis; Colorimetry; Metal Nanoparticles
PubMed: 36615266
DOI: 10.3390/molecules28010070 -
Mikrochimica Acta Jul 2022The pathway from the advanced electrocatalyst to nanozymes defeating natural enzyme is reviewed. Prussian blue, being the most advantageous electrocatalyst for... (Review)
Review
The pathway from the advanced electrocatalyst to nanozymes defeating natural enzyme is reviewed. Prussian blue, being the most advantageous electrocatalyst for hydrogen peroxide reduction, is obviously the best candidate for mimicking peroxidase activity. Indeed, catalytically synthesized Prussian blue nanoparticles are characterized by the catalytic rate constants, which are significantly (up to 4 orders of magnitude) higher than for enzyme peroxidase. Displaying in addition the enzymatic specificity in terms of an absence of oxidase-like activity, catalytically synthesized Prussian blue nanoparticles can be referred to as nanozymes. The latter provide the most versatile method for surface covering with the electrocatalyst, allowing to modify non-traditional materials like boron-doped diamond. For stabilization, Prussian blue core can be covered with nickel hexacyanoferrate shell; the resulting core-shell nanozymes still defeat natural enzyme in terms of activity. Discovering the catalytic pathway of nanozymes "artificial peroxidase" action, we have found the novel advantage of nanozymes over the corresponding biological catalysts: their dramatically (100 times) improved bimolecular rate constants.
Topics: Catalysis; Ferrocyanides; Nanoparticles; Peroxidase; Peroxidases
PubMed: 35879483
DOI: 10.1007/s00604-022-05363-w -
Food Chemistry Mar 2022In the present study, we investigated the impacts of ultrasonic conditions on the phytochemical profiles, antioxidant activity, and polyphenol oxidase (PPO) and...
In the present study, we investigated the impacts of ultrasonic conditions on the phytochemical profiles, antioxidant activity, and polyphenol oxidase (PPO) and peroxidase (POD) activities in coffee leaves. Ultrasonic frequency, power, and time, pH, and incubation time affected PPO and POD differently, thus resulting in different ABTS scavenging capacity and phenolic content in coffee leaves. Triple-frequency (20/35/50 kHz) ultrasound significantly (P < 0.05) inhibited trigonelline, caffeine, mangiferin, rutin, chlorogenic acids, antioxidant activity, and PPO activity, while the single frequency of 35 kHz increased the phenolics compounds, which was associated with the lowest POD activity. Increasing the incubation time after ultrasonication gradually decreased phenolic compounds and antioxidant activities, however, POD activity followed a temporal pattern of first increase and then decrease. Our results showed that PPO and POD were temporally inactivated after ultrasonication, which leading to the continuous decrease of phenolics in coffee leaves.
Topics: Antioxidants; Catechol Oxidase; Coffee; Peroxidase; Peroxidases; Phytochemicals; Plant Leaves
PubMed: 34731790
DOI: 10.1016/j.foodchem.2021.131480