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Peroxidase

Peroxidases are a superfamily of oxidoreductase enzymes (EC 1.11.1.x) that catalyze the reduction of hydrogen peroxide (H₂O₂) or other peroxides using a variety of electron-donating substrates, thereby facilitating the oxidation of diverse organic and inorganic compounds.^[1] These enzymes are ubiquitous across plants, animals, and microorganisms, where they primarily function to mitigate oxidative stress by detoxifying reactive oxygen species (ROS), although they also participate in biosynthetic pathways, pathogen defense, and hormone regulation.^[1]^[2] Peroxidases are broadly classified into two main groups: heme-containing peroxidases, which account for approximately 80% of known types and rely on a prosthetic heme group for catalysis, and non-heme peroxidases, which utilize alternative redox centers such as selenium, manganese, or cysteine thiols.^[1]^[2] Heme peroxidases are further subdivided into superfamilies, including the peroxidase-catalase (PCAT) family with three classes—Class I (intracellular, e.g., cytochrome c peroxidase in eukaryotes), Class II (secretory fungal enzymes like lignin peroxidase and manganese peroxidase), and Class III (plant-specific extracellular enzymes such as horseradish peroxidase)—the peroxidase-cyclooxygenase (PCOXS) superfamily, and the dye-decolorizing peroxidase (DyP)-type superfamily, primarily found in bacteria and fungi.^[1]^[2]^[3] Non-heme examples include glutathione peroxidases (GPx), which incorporate selenocysteine for antioxidant activity.^[1]^[2] Structurally, heme peroxidases typically consist of glycoproteins with molecular masses of 30–60 kDa, featuring a conserved heme b prosthetic group where the iron atom is axially ligated by a histidine residue, enabling a catalytic cycle that involves compound I and II intermediates for sequential one-electron transfers.^[4]^[1] Many also contain disulfide bridges and calcium ions for structural stability, particularly in Classes II and III, while non-heme peroxidases exhibit more varied architectures, such as the dimeric or tetrameric forms in peroxiredoxins with catalytic cysteine or selenocysteine residues.^[2]^[4] Biologically, peroxidases perform essential roles tailored to their host organisms: in plants, Class III enzymes contribute to cell wall lignification, suberization, and wound healing; in animals, myeloperoxidase generates hypochlorous acid for antimicrobial activity in neutrophils, while GPx protects against lipid peroxidation; and in microbes, versatile peroxidases aid in lignin degradation and environmental adaptation.^[1]^[2] Beyond their natural functions, peroxidases have garnered attention for biotechnological applications, including bioremediation of pollutants, decolorization of industrial dyes, pulp bleaching, wastewater treatment, and development of biosensors, owing to their high specificity, stability under extreme conditions, and ease of immobilization on nanostructures for enhanced reusability.^[1]^[2]

Fundamentals

Catalytic Reaction

Peroxidases catalyze the reduction of peroxides by electron donors, facilitating the breakdown of reactive oxygen species in biological systems. The general reaction catalyzed by these enzymes is:

\text{ROOR'} + 2e^- + 2H^+ \rightarrow \text{ROH} + \text{R'OH}

where ROOR' represents a peroxide substrate such as hydrogen peroxide (H₂O₂).^[5] This two-electron reduction process protects cells from oxidative damage by converting peroxides into less reactive alcohols.^[6] For hydrogen peroxide specifically, the reaction can be expressed as:

\text{H}_2\text{O}_2 + 2\text{AH} \rightarrow 2\text{H}_2\text{O} + 2\text{A}

where AH denotes the reducing substrate that donates electrons.^[7] This equation highlights the enzyme's role in detoxifying H₂O₂, a common byproduct of aerobic metabolism.^[7] The catalytic cycle operates through a two-phase mechanism characteristic of many peroxidases. In the first phase, the resting ferric (Fe(III)) form of the enzyme binds the peroxide, leading to heterolytic cleavage of the O-O bond and formation of Compound I, an active intermediate consisting of an oxyferryl heme (Fe(IV)=O) and a porphyrin π-cation radical.^[8] This step is facilitated by proton transfers involving distal residues, resulting in a highly oxidizing species capable of abstracting electrons.^[8] In the second phase, Compound I undergoes two sequential one-electron reductions by the donor substrate: the first yields Compound II (Fe(IV)=O without the radical), and the second restores the enzyme to its ferric resting state.^[7] This ping-pong mechanism ensures efficient turnover while minimizing free radical leakage.^[6] Heme-containing peroxidases exemplify this process, relying on the iron-porphyrin cofactor for redox activity.^[8] The efficiency of peroxidase catalysis is critically influenced by the redox potentials of the enzyme's intermediates, particularly those of Compound I and Compound II relative to the donor substrate. These potentials dictate the thermodynamic driving force for electron transfer, with higher enzyme potentials enabling oxidation of substrates with more positive reduction potentials, as described by Marcus theory.^[9] Variations in these potentials across peroxidase classes can limit or enhance catalytic rates, with engineering efforts often targeting them to broaden substrate specificity.^[9]

Substrates and Cofactors

Peroxidases primarily utilize hydrogen peroxide (H₂O₂) as their optimal inorganic substrate, serving as the oxidant that facilitates the reduction process in their catalytic activity.^[10] Organic hydroperoxides, such as alkyl hydroperoxides (ROOH), also function as effective substrates, enabling the enzyme to reduce these compounds to corresponding alcohols while oxidizing secondary donors.^[6] The enzymes demonstrate broad specificity for electron donors, with many peroxidases oxidizing versatile substrates including phenols and anilines, which are common in microbial and animal-derived isoforms.^[1] In contrast, certain plant peroxidases exhibit higher specificity toward substrates like guaiacol, reflecting adaptations to lignification processes.^[1] Heme, composed of iron-protoporphyrin IX, serves as the essential cofactor in the majority of peroxidases, coordinating the iron atom at the active site to enable peroxide binding and electron transfer.^[6] Glutathione peroxidases, however, rely on non-heme cofactors such as redox-active cysteine or selenocysteine residues, which directly participate in peroxide reduction without a porphyrin prosthetic group.^[10] Haloperoxidases incorporate vanadium as their key inorganic cofactor, facilitating halide oxidation in the presence of peroxides.^[11] Cyanide acts as a potent inhibitor of heme-containing peroxidases by binding tightly to the ferric iron in the heme group, thereby occupying the axial coordination site and preventing substrate access.^[12]

Classification and Diversity

Major Classes

Peroxidases are classified under the Enzyme Commission (EC) number 1.11.1.x, encompassing oxidoreductases that catalyze the reduction of hydrogen peroxide (H₂O₂) or organic hydroperoxides using electron donors such as AH₂, following the general reaction H₂O₂ + 2AH₂ → 2H₂O + 2A.^[13] This classification highlights their role in peroxide detoxification and oxidation processes across diverse organisms.^[14] Heme-containing peroxidases, which utilize heme as a prosthetic group, are traditionally divided into three structural classes based on amino acid sequence similarities, cellular localization, and taxonomic distribution.^[15] Class I peroxidases are intracellular enzymes primarily found in prokaryotes and lower eukaryotes, including catalase-peroxidases (EC 1.11.1.6) from bacteria like Mycobacterium tuberculosis and ascorbate peroxidase (EC 1.11.1.11) from plants and algae.^[1] These enzymes often feature a single domain with conserved histidine and aspartate residues coordinating the heme iron.^[16] Class II peroxidases are typically secretory and occur in fungi, exemplified by lignin peroxidase (EC 1.11.1.14) in wood-degrading fungi like Phanerochaete chrysosporium.^[1] Class III peroxidases are exclusive to plants and function extracellularly, with horseradish peroxidase (EC 1.11.1.7) from Armoracia rusticana serving as a prototypical example; these enzymes possess two calcium-binding sites that stabilize their structure.^[1] Heme peroxidases also include the peroxidase-cyclooxygenase (PCOXS) superfamily, primarily found in animals, which encompasses enzymes like myeloperoxidase (EC 1.11.1.7) in mammalian neutrophils and lactoperoxidase in exocrine glands. These enzymes feature distinct structural motifs, such as a covalent heme linkage, enabling halide oxidation and antimicrobial activity.^[15] Beyond the heme-based classes, non-heme peroxidases include several variants adapted to specific redox environments across all kingdoms of life. Peroxiredoxins (e.g., EC 1.11.1.15) are thiol-dependent enzymes that reduce peroxides using thioredoxin or glutaredoxin as electron donors, forming disulfide bonds in their catalytic cysteine residues during the reaction cycle.^[17] Glutathione peroxidases (GPx; e.g., EC 1.11.1.9) utilize glutathione as a reductant and often incorporate selenocysteine at the active site in animals for enhanced activity.^[1] Dye-decolorizing peroxidases (DyP; EC 1.11.1.19) are heme-containing but distinct, known for their ability to oxidize high-redox-potential substrates like dyes and manganese.^[1] Haloperoxidases (e.g., EC 1.11.1.10) incorporate halides into organic substrates using peroxide, with vanadium-containing variants prevalent in marine algae and bacteria.^[17] The RedoxiBase database provides a centralized resource for peroxidase research, compiling over 15,000 annotated sequences from more than 2,599 organisms as of April 2019, including both heme and non-heme types, to facilitate comparative analysis and identification of conserved motifs.^[18]

Evolutionary Origins

Peroxidases trace their origins to ancient prokaryotic lineages, primarily in bacteria and archaea, where they evolved as essential enzymes for detoxifying reactive oxygen species (ROS) generated during early metabolic processes. These primordial peroxidases, such as those in the peroxidase–cyclooxygenase superfamily, are evident in cyanobacteria and other prokaryotes, functioning to mitigate oxidative stress in oxygen-scarce environments.^[19] Their emergence is closely tied to the rise of oxygenic photosynthesis, with fossil and molecular evidence suggesting that short peroxicins in cyanobacteria represent some of the earliest heme peroxidases adapted for ROS management.^[19] Horizontal gene transfer played a pivotal role in disseminating peroxidase genes from prokaryotes to eukaryotes, enabling the latter to cope with increasing atmospheric oxygen levels. For instance, genes encoding DyP-type peroxidases were transferred from cyanobacteria to fungi, while other peroxidase variants moved to early eukaryotic lineages, facilitating adaptation across domains of life.^[19] This transfer is supported by phylogenetic analyses showing non-vertical inheritance patterns in diverse taxa.^[20] Key structural elements, such as heme-binding motifs involving histidine or cysteine ligation, have been remarkably conserved from bacterial ancestors to mammalian descendants, underscoring the enzymes' fundamental role in redox homeostasis.^[19] In the case of glutathione peroxidases (GPxs), a eukaryotic innovation involves the incorporation of selenocysteine at the active site, encoded by a TGA codon unique to metazoan lineages, which enhances catalytic efficiency against peroxides.^[20] The diversification of peroxidases accelerated through gene duplication events, leading to multiple isoforms tailored to specific niches; for example, humans possess eight GPx genes (GPx1–7 and NPGPx) arising from duplications of a common ancestral sequence, with splits like GPx1/2 predating the divergence of birds and mammals.^[20] This expansion correlates with the Great Oxidation Event approximately 2.4 billion years ago, when rising oxygen levels—driven by cyanobacterial activity—necessitated robust antioxidant defenses, as evidenced by the proliferation of prokaryotic peroxidase variants in the geological record.^[19]

Structural Features

Molecular Architecture

Heme-containing peroxidases are globular proteins characterized by a conserved overall fold that incorporates a hydrophobic pocket for the prosthetic heme group. This architecture positions the heme b (iron-protoporphyrin IX) in a manner that allows access to the distal edge for substrate interaction while shielding the proximal side. In the peroxidase-catalase superfamily, which includes class II and III peroxidases, the fold is predominantly alpha-helical, comprising approximately 12 helices that form a compact globular domain, providing structural stability and defining the heme environment.^[19] The active site is centered on the heme iron, which in the resting ferric state is coordinated by a proximal histidine residue serving as the fifth axial ligand, often stabilized through hydrogen bonding to a nearby aspartate or similar residue. This proximal ligation tunes the iron's redox potential and facilitates electron transfer during catalysis. On the distal side, a conserved histidine, typically assisted by an arginine via a hydrogen-bonded triad (often involving a tryptophan or phenylalanine), acts as a general acid-base catalyst to promote the heterolytic O-O bond cleavage of hydrogen peroxide, leading to the formation of Compound I. These features are common across the peroxidase-catalase superfamily and essential for the enzyme's oxidative mechanism.^[19]^[21] Peroxidases assemble into various oligomeric states, ranging from monomers to dimers and tetramers, with oligomerization often mediated by hydrophobic and electrostatic interactions at subunit interfaces to enhance thermal stability or regulate access to the active site. Spectroscopically, the ferric state of these enzymes exhibits a characteristic Soret absorption band at approximately 400 nm, reflecting the penta-coordinate heme geometry; this band undergoes red or blue shifts (e.g., to 420 nm in Compound II) upon substrate binding or intermediate formation, providing a diagnostic signature of the heme's electronic perturbations.^[22]^[23]

Key Examples

Horseradish peroxidase (HRP), a representative class III peroxidase from plants, comprises a single polypeptide chain of 308 amino acid residues and is extensively glycosylated, with carbohydrates accounting for about 18% of its molecular weight.^[24] The crystal structure (PDB: 1ATJ) displays a compact globular fold dominated by α-helices surrounding a covalently attached heme group, with four disulfide bridges and two calcium ions stabilizing the architecture; this heme pocket configuration enables a versatile substrate range by accommodating diverse phenolic and aromatic compounds. In contrast, myeloperoxidase (MPO), a mammalian heme peroxidase, forms a homodimeric structure with each ~150 kDa subunit featuring a bisected heavy and light chain linked by a disulfide bond, and its distinctive green coloration arises from a modified chlorin-type heme covalently bound via unique autopeptide linkages. Crystal structures, such as PDB: 1MHL, reveal two calcium-binding sites per subunit that contribute to structural integrity and flexibility, while the distal heme cavity includes a halogenation site with histidine and arginine residues poised for chloride oxidation. Glutathione peroxidase 1 (GPx1), exemplifying non-heme selenoperoxidases, assembles as a tetramer with each subunit containing a selenocysteine residue at the active site, diverging markedly from heme-based architectures by relying on selenium-thiol chemistry for catalysis.^[25] The refined structure (PDB: 1GP1) shows a β-sheet-rich fold with the catalytic Sec46 buried in a shallow groove, allowing access for glutathione substrates and highlighting a mechanism independent of iron protoporphyrin. Lignin peroxidase (LiP), a fungal class II peroxidase, adopts a helical heme-containing fold similar to plant peroxidases but distinguished by a surface-exposed tryptophan radical site essential for long-range electron transfer. The high-resolution structure (PDB: 1LLP) of the Phanerochaete chrysosporium enzyme reveals a hydroxylated Trp171 at the Cβ position, which facilitates oxidation of recalcitrant substrates like veratryl alcohol through radical propagation from the heme.^[26]

Biological Roles

In Plants and Microbes

In plants, class III peroxidases play crucial roles in defense mechanisms, particularly through lignification and suberization processes that fortify cell walls against pathogen invasion.^[27] These enzymes catalyze the oxidative polymerization of monolignols into lignin, creating a physical barrier that restricts microbial penetration, while suberization involves the deposition of suberin-polyphenolic domains in response to wounding or infection.^[28] For instance, in the Solanaceae family, guaiacol peroxidase activity is significantly upregulated in resistant tomato cultivars (Solanum lycopersicum) upon infection by Ralstonia solanacearum, enhancing oxidative burst and contributing to bacterial wilt resistance compared to susceptible varieties.^[29] Additionally, class III peroxidases participate in reactive oxygen species (ROS) signaling by balancing hydrogen peroxide (H₂O₂) levels in the apoplast, which facilitates cell wall crosslinking via phenolic dimerization during wounding responses, thereby promoting tissue repair and defense.00221-3) In microbes, peroxidases enable adaptation to oxidative stress and environmental niches. Catalase-peroxidases, such as KatG in Mycobacterium tuberculosis, confer resistance to H₂O₂ by decomposing it and neutralizing organic peroxides, allowing survival within host phagocytes and contributing to pathogenesis.^[30] Haloperoxidases in marine algae, including vanadium-dependent bromoperoxidases, catalyze the bromination of organic substrates using H₂O₂ and bromide ions, leading to the production of halogenated metabolites that deter herbivores and facilitate ecological interactions in marine environments.^[31] In fungi, lignin peroxidases secreted by white-rot species like Phanerochaete chrysosporium enable the degradation of lignocellulosic materials in wood, breaking down recalcitrant lignin through high-redox-potential oxidation and supporting nutrient recycling in forest ecosystems.^[32]

In Animals and Humans

In animals and humans, peroxidases play crucial roles in cellular protection, immune defense, and hormone biosynthesis. Glutathione peroxidases (GPxs) are key selenoproteins involved in antioxidant defense, where they catalyze the reduction of hydrogen peroxide and lipid hydroperoxides using glutathione as a cofactor, thereby preventing oxidative damage to membranes and biomolecules. There are eight GPx isoforms in humans (GPx1–GPx8), with GPx1 being the most abundant and ubiquitously expressed, incorporating selenium at its active site for enhanced catalytic efficiency in detoxifying reactive oxygen species during metabolism. These enzymes are particularly vital in tissues prone to oxidative stress, such as the brain and cardiovascular system, where they maintain redox homeostasis. Peroxidases also contribute significantly to innate immunity in animals. Myeloperoxidase (MPO), highly concentrated in neutrophil granules, utilizes hydrogen peroxide generated during the respiratory burst to oxidize chloride ions, producing hypochlorous acid (HOCl), a potent antimicrobial agent that effectively kills engulfed bacteria and fungi. This mechanism is essential for the rapid clearance of pathogens during infections, with MPO accounting for up to 5% of the dry weight of neutrophils in humans and other mammals. Similarly, lactoperoxidase (LPO), found in exocrine secretions like saliva and milk, oxidizes thiocyanate to hypothiocyanite (OSCN⁻) in the presence of hydrogen peroxide, exerting broad-spectrum antimicrobial effects against oral and gastrointestinal bacteria while being non-toxic to host cells. In thyroid physiology, thyroid peroxidase (TPO) is indispensable for hormone synthesis, catalyzing the iodination of tyrosine residues on thyroglobulin and the subsequent coupling to form thyroxine (T4) and triiodothyronine (T3), which regulate metabolism across vertebrate species. Dysregulation of TPO is implicated in autoimmune disorders, notably Hashimoto's thyroiditis, where autoantibodies against TPO (anti-TPO) are present in over 90% of patients, leading to glandular destruction and hypothyroidism. These antibodies interfere with TPO's enzymatic activity and contribute to chronic inflammation, highlighting the enzyme's dual role in endocrine function and autoimmunity. Associations between peroxidase dysregulation and disease underscore their clinical relevance. Elevated circulating MPO levels serve as a biomarker for cardiovascular disease risk, correlating with atherosclerosis progression, endothelial dysfunction, and adverse events in conditions like acute coronary syndrome due to MPO-mediated oxidative modification of lipoproteins. Deficiencies or reduced activity in GPx isoforms, such as GPx1 and GPx4, are linked to neurodegeneration, exacerbating oxidative stress and ferroptosis in disorders like Parkinson's and Alzheimer's disease, where impaired peroxide detoxification accelerates neuronal loss.

Applications

Industrial and Environmental

Peroxidases play a significant role in industrial wastewater treatment, particularly through the enzymatic polymerization of phenolic compounds into insoluble products that can be easily removed. Horseradish peroxidase (HRP), a widely studied enzyme, catalyzes the oxidation of phenols in the presence of hydrogen peroxide (H₂O₂), leading to the formation of polymeric precipitates that effectively reduce phenol concentrations in effluents from industries such as petroleum refining and manufacturing.^[33] This process operates under mild conditions (pH 5–9 and temperatures 5–50°C), offering an environmentally friendly alternative to chemical treatments, with studies demonstrating up to 93% phenol removal in spiked wastewater samples.^[34] Immobilized HRP variants enhance enzyme stability and reusability, enabling continuous treatment systems for large-scale applications.^[35] In polymer synthesis, peroxidases facilitate the oxidative coupling of monomers to produce materials used in adhesives, coatings, and biofuel cells. For instance, HRP and other peroxidases catalyze the polymerization of aniline into conductive polyaniline, a polymer valued for its electrical properties in coatings and electronic components.^[36] Enzymatic methods using peroxidases enable milder reaction conditions compared to traditional chemical synthesis, reducing energy use and environmental impact while yielding polymers with controlled structures for adhesive formulations.^[37] In biofuel cells, peroxidases such as HRP serve as biocatalysts at the cathode, reducing H₂O₂ to generate electrical power, with hybrid systems achieving open-circuit voltages up to 1.68 V.^[38] Peroxidases contribute to the food industry through applications such as protein crosslinking in baking processes, enhancing dough properties and product texture.^[39] Immobilized enzyme systems improve efficiency in industrial-scale operations.^[40] For environmental remediation, microbial peroxidases, including dye-decolorizing peroxidases (DyPs), are employed to break down synthetic dyes in textile wastewater, converting them into less toxic compounds through oxidative cleavage. Bacterial DyPs exhibit broad substrate specificity and stability in harsh conditions, achieving high decolorization rates (up to 90%) for azo and anthraquinone dyes under neutral pH. Recent advances in unspecific peroxygenases (UPOs), a class of fungal heme-thiolate peroxidases, have expanded their utility in organic synthesis for remediation-inspired processes; for example, in 2024, UPOs were shown to catalyze the formation of azoxy compounds from anilines, enabling selective oxidation pathways for pollutant degradation.^[41] These developments, including enzyme cascades for in situ H₂O₂ generation, address stability challenges and promote scalable applications in sustainable synthesis.^[42]

Biomedical and Diagnostic

Peroxidases play a pivotal role in biomedical diagnostics, particularly through horseradish peroxidase (HRP), which is widely employed in enzyme-linked immunosorbent assays (ELISA) for sensitive detection of biomolecules. In ELISA protocols, HRP serves as a reporter enzyme conjugated to antibodies, catalyzing the oxidation of chromogenic substrates such as 3,3',5,5'-tetramethylbenzidine (TMB) in the presence of hydrogen peroxide to produce a colored product that amplifies the signal for quantification via spectrophotometry. This approach enables the detection of analytes at picomolar concentrations, making it essential for clinical tests like those for infectious diseases, hormones, and tumor markers. HRP's stability and high turnover rate have made it one of the most commonly used enzymes in commercial ELISA kits, particularly in histochemistry and immunoassay formats.^[43]^[44] In therapeutic contexts, peroxidase inhibitors and mimetics target oxidative stress and inflammation associated with various diseases. Myeloperoxidase (MPO), a human peroxidase abundant in neutrophils, contributes to chronic inflammation by generating hypochlorous acid and other oxidants that exacerbate conditions like cardiovascular disease and atherosclerosis; inhibitors such as AZD4831 have shown promise in preclinical models by reducing endothelial dysfunction and vascular inflammation without affecting MPO's antimicrobial roles. Similarly, glutathione peroxidase (GPx) mimetics, such as ebselen, emulate the enzyme's antioxidant function by reducing peroxides and mitigating oxidative damage in pathologies like neurodegenerative disorders and ischemia-reperfusion injury, with ongoing phase II clinical trials demonstrating efficacy in conditions involving redox imbalance. These strategies leverage peroxidases' roles in innate immunity, where MPO aids pathogen clearance, to selectively modulate harmful oxidative signaling.^[45]^[46]^[47]^[48] Peroxidase-like nanozymes have emerged as robust alternatives to natural enzymes in biosensors, offering enhanced stability and cost-effectiveness for point-of-care diagnostics. Copper oxide (CuO) nanoparticles exhibit intrinsic peroxidase-mimicking activity, catalyzing the oxidation of substrates like TMB to detect glucose through colorimetric changes, with studies reporting detection limits in the low micromolar range in complex biological samples such as blood or urine. These nanozymes, often integrated into graphene-based composites, enable portable devices for diabetes monitoring by coupling glucose oxidase reactions with the peroxidase-like cascade, achieving selectivity over interferents like ascorbic acid. As of 2025, advances in 2D nanomaterial-based peroxidase mimics have further improved biosensing for pollutants and biomarkers. Such innovations address limitations of protein-based peroxidases, like HRP, by resisting denaturation in harsh environments.^[49]^[50]^[51] Recent advances highlight peroxidases' potential in targeted therapies and synthetic biology. Peroxiredoxins (Prxs), a family of non-seleno peroxidases, regulate cancer redox signaling by scavenging peroxides and modulating pathways like NF-κB and HIF-1α; 2024 research on peroxiredoxin-1 and -2 in cervical cancer cells demonstrated that their inhibition enhances bleomycin efficacy by disrupting tumor survival signals, suggesting Prxs as adjuvant targets in redox-directed chemotherapy. In drug synthesis, unspecific peroxygenases (UPOs) enable selective C-H oxygenation for metabolite production, with 2024 studies showcasing fungal UPOs in forming azoxy compounds from anilines—key intermediates in pharmaceuticals—via peroxide-driven mechanisms that outperform traditional chemical routes in stereoselectivity and mild conditions. These developments underscore peroxidases' expanding utility in precision medicine and biocatalytic drug design.^[52]^[41]^[53]

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(PDF) Use of Immobilised Catalase to Remove H2O2 Used in the ...
Aug 6, 2025 · The removal of H2O2 used in milk sterilisation was accomplished by catalase immobilised on DEAE-cellulose, modified initially with 2-amino-4,6- ...
[40]
Unspecific peroxygenase enabled formation of azoxy compounds
Sep 27, 2024 · In this study, we discovered that fungal unspecific peroxygenases are promising catalysts for synthesizing azoxy products from simple aniline starting ...
[41]
Constant Enzymatic in situ Production of H2O2 for an Unspecific ...
Mar 17, 2025 · We developed an enzyme cascade with an l-amino acid oxidase (LAAO) to produce hydrogen peroxide in situ at a constant low concentration.
[42]
Enzyme Linked Immunosorbent Assay - StatPearls - NCBI Bookshelf
However, the substrates most commonly used are horseradish peroxidase (HRP) and alkaline phosphatase (AP).[3] The substrate for HRP is hydrogen peroxide, ...
[43]
An updated view on horseradish peroxidases: recombinant ... - NIH
When the gene structures of 73 class III peroxidases from the model plant Arabidopsis thaliana were studied, a conserved exon/intron structure of four exons ...
[44]
Discovery of AZD4831, a Mechanism-Based Irreversible Inhibitor of ...
Aug 25, 2022 · Myeloperoxidase is a promising therapeutic target for treatment of patients suffering from heart failure with preserved ejection fraction ...<|separator|>
[45]
Inhibition of MPO (Myeloperoxidase) Attenuates Endothelial ...
May 2, 2019 · Pharmacological inhibition of MPO is a potential strategy to limit endothelial dysfunction in vascular inflammation.
[46]
Targeting oxidative stress in disease: promise and limitations of ...
Jun 30, 2021 · Currently, there are clinical trials ongoing for ebselen, a glutathione peroxidase (GPX) mimic, for Meniere disease in phase II (NCT02603081); ...
[47]
Targeting Myeloperoxidase (MPO) Mediated Oxidative Stress and ...
This article discusses the important roles of MPO in mediating oxidative stress and neuroinflammation during cerebral ischemia-reperfusion injury.
[48]
A Highly Stable Graphene‐Based Metal Oxide Nano Enzyme with ...
May 15, 2023 · The CuO/3D(N)GFs nanozyme, made of graphene and metal oxide, is used for equipment-free, one-step diagnosis of diabetes by measuring glucose ...
[49]
Cu0.89Zn0.11O, A New Peroxidase-Mimicking Nanozyme with High ...
The nanozyme, when tested for the detection of glucose, showed a substantial enhancement in the detection selectivity.
[50]
Peroxiredoxin I and II as novel therapeutic molecular targets in ...
May 31, 2024 · This research highlights the importance of PRDX1 and 2 in cervical cancer treatments with bleomycin, showing their potential to enhance treatment efficacy.
[51]
Challenges and perspectives in using unspecific peroxygenases for ...
Oct 14, 2024 · This review article provides a concrete and mini-overview of the challenges associated with using UPOs in organic synthesis and discusses strategies for enzyme ...