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The Tohoku Journal of Experimental... 1953
Topics: Hormones; Liver; Oxidoreductases; Peroxidase; Peroxidases
PubMed: 13136141
DOI: 10.1620/tjem.58.112 -
IUBMB Life May 2022Hemoglobin oxidation due to oxidative stress and disease conditions leads to the generation of ROS (reactive oxygen species) and membrane attachment of hemoglobin...
Hemoglobin oxidation due to oxidative stress and disease conditions leads to the generation of ROS (reactive oxygen species) and membrane attachment of hemoglobin in-vivo, where its redox activity leads to peroxidative damage of membrane lipids and proteins. Spectrin, the major component of the red blood cell (RBC) membrane skeleton, is known to interact with hemoglobin and, here this interaction is shown to increase hemoglobin peroxidase activity in the presence of reducing substrate ABTS (2', 2'-Azino-Bis-3-Ethylbenzothiazoline-6-Sulfonic Acid). It is also shown that in the absence of reducing substrate, spectrin forms covalently cross-linked aggregates with hemoglobin which display no peroxidase activity. This may have implications in the clearance of ROS and limiting peroxidative damage. Spectrin is found to modulate the peroxidase activity of different hemoglobin variants like A, E, and S, and of isolated globin chains from each of these variants. This may be of importance in disease states like sickle cell disease and HbE-β-thalassemia, where increased oxidative damage and free globin subunits are present due to the defects inherent in the hemoglobin variants associated with these diseases. This hypothesis is corroborated by lipid peroxidation experiments. The modulatory role of spectrin is shown to extend to other heme proteins, namely catalase and cytochrome-c. Experiments with free heme and Raman spectroscopy of heme proteins in the presence of spectrin show that structural alterations occur in the heme moiety of the heme proteins on spectrin binding, which may be the structural basis of increased enzyme activity.
Topics: Antioxidants; Catalase; Heme; Hemeproteins; Hemoglobins; Peroxidase; Peroxidases; Reactive Oxygen Species; Spectrin
PubMed: 35184374
DOI: 10.1002/iub.2607 -
Applied Microbiology and Biotechnology May 2021Aryl-alcohol oxidases (AAOs) are FAD-containing enzymes that oxidize a broad range of aromatic as well as aliphatic allylic alcohols to aldehydes. Their broad substrate... (Review)
Review
Aryl-alcohol oxidases (AAOs) are FAD-containing enzymes that oxidize a broad range of aromatic as well as aliphatic allylic alcohols to aldehydes. Their broad substrate spectrum accompanied by the only need for molecular oxygen as cosubstrate and production of hydrogen peroxide as sole by-product makes these enzymes very promising biocatalysts. AAOs were used in the synthesis of flavors, fragrances, and other high-value-added compounds and building blocks as well as in dye decolorization and pulp biobleaching. Furthermore, AAOs offer a huge potential as efficient suppliers of hydrogen peroxide for peroxidase- and peroxygenase-catalyzed reactions. A prerequisite for application as biocatalysts at larger scale is the production of AAOs in sufficient amounts. Heterologous expression of these predominantly fungal enzymes is, however, quite challenging. This review summarizes different approaches aiming at enhancing heterologous expression of AAOs and gives an update on substrates accepted by these promising enzymes as well as potential fields of their application. KEY POINTS: • Aryl-alcohol oxidases (AAOs) supply ligninolytic peroxidases with HO. • AAOs accept a broad spectrum of aromatic and aliphatic allylic alcohols. • AAOs are potential biocatalysts for the production of high-value-added bio-based chemicals.
Topics: Alcohol Oxidoreductases; Alcohols; Fungi; Hydrogen Peroxide; Lignin; Peroxidase; Peroxidases
PubMed: 33997930
DOI: 10.1007/s00253-021-11337-4 -
Redox Biology May 2020Cytoglobin is an evolutionary ancient hemoglobin with poor functional annotation. Rather than constrained to penta coordination, cytoglobin's heme iron may exist either... (Review)
Review
Cytoglobin is an evolutionary ancient hemoglobin with poor functional annotation. Rather than constrained to penta coordination, cytoglobin's heme iron may exist either as a penta or hexacoordinated arrangement when exposed to different intracellular environments. Two cysteine residues at the surface of the protein form an intramolecular disulfide bond that regulates iron coordination, ligand binding, and peroxidase activity. Overall, biochemical results do not support a role for cytoglobin as a direct antioxidant enzyme that scavenges hydrogen peroxide because the rate of the reaction of cytoglobin with hydrogen peroxide is several orders of magnitude slower than metal and thiol-based peroxidases. Thus, alternative substrates such as fatty acids have been suggested and regulation of nitric oxide bioavailability through nitric oxide dioxygenase and nitrite reductase activities has received experimental support. Cytoglobin is broadly expressed in connective, muscle, and nervous tissues. Rational for differential cellular distribution is poorly understood but inducibility in response to hypoxia is one of the most established features of cytoglobin expression with regulation through the transcription factor hypoxia-inducible factor (HIF). Phenotypic characterization of cytoglobin deletion in the mouse have indicated broad changes that include a heightened inflammatory response and fibrosis, increase tumor burden, cardiovascular dysfunction, and hallmarks of senescence. Some of these changes might be reversed upon inhibition of nitric oxide synthase. However, subcellular and molecular interactions have been seldom characterized. In addition, specific molecular mechanisms of action are still lacking. We speculate that cytoglobin functionality will extend beyond nitric oxide handling and will have to encompass indirect regulatory antioxidant and redox sensing functions.
Topics: Animals; Cytoglobin; Globins; Mice; Oxygenases; Peroxidase; Peroxidases
PubMed: 32087552
DOI: 10.1016/j.redox.2020.101468 -
Food Research International (Ottawa,... May 2021Peroxidase is an enzyme in the group of oxidoreductases that is widely distributed in nature. It can catalyze the oxidation of various organic and inorganic substrates... (Review)
Review
Peroxidase is an enzyme in the group of oxidoreductases that is widely distributed in nature. It can catalyze the oxidation of various organic and inorganic substrates by reacting with hydrogen peroxide and similar molecules. Due to its wide catalytic activity, peroxidases can act in the removal of both phenolic compounds and peroxides, in chemical synthesis and, according to recent studies, in mycotoxin degradation. Therefore, this study aimed at introducing an overview of the mechanism of peroxidase action, extraction sources, mycotoxin degradation capacity and other potential applications in the food industry.
Topics: Oxidation-Reduction; Oxidoreductases; Peroxidase; Peroxidases; Phenols
PubMed: 33992367
DOI: 10.1016/j.foodres.2021.110266 -
Molecules (Basel, Switzerland) Dec 2016'Nanozymes', a term coined by Scrimin, Pasquato, and co-workers to describe nanomaterials with enzyme-like characteristics, represent an exciting and emerging research... (Review)
Review
'Nanozymes', a term coined by Scrimin, Pasquato, and co-workers to describe nanomaterials with enzyme-like characteristics, represent an exciting and emerging research area in the field of artificial enzymes. Indubitably, the last decade has witnessed substantial advancements in the design of a variety of functional nanoscale materials, including metal oxides and carbon-based nanomaterials, which mimic the structures and functions of naturally occurring enzymes. Among these, carbon nanodots (C-dots) or carbon quantum dots (CQDs) offer huge potential due to their unique properties as compared to natural enzymes and/or classical artificial enzymes. In this mini review, we discuss the peroxidase-like catalytic activities of C-dots and their applications in biosensing. The scope intends to cover not only the C-dots but also graphene quantum dots (GQDs), doped C-dots/GQDs, carbon nitride dots, and C-dots/GQDs nanocomposites. Nevertheless, this mini review is designed to be illustrative, not comprehensive.
Topics: Biomimetic Materials; Biosensing Techniques; Carbon; Graphite; Nanocomposites; Peroxidase; Quantum Dots
PubMed: 27918453
DOI: 10.3390/molecules21121653 -
Biochemical Society Transactions Oct 2023Peroxidasin is a heme-containing peroxidase enzyme that plays a vital role in the cross-linking of collagen IV molecules in basement membranes. Collagen IV cross-links... (Review)
Review
Peroxidasin is a heme-containing peroxidase enzyme that plays a vital role in the cross-linking of collagen IV molecules in basement membranes. Collagen IV cross-links are essential for providing structure and mechanical stability throughout tissue development, homeostasis, and wound healing. During cancer progression, the basement membrane is degraded, and proteins typically found in the basement membrane, including peroxidasin and collagen IV, can be found spread throughout the tumour microenvironment where they interact with cancer cells and alter cell behaviour. Whilst peroxidasin is reported to be up-regulated in a number of different cancers, the role that it plays in disease progression and metastasis has only recently begun to be studied. This review highlights the current literature exploring the known roles of peroxidasin in normal tissues and cancer progression, regulators of peroxidasin expression, and the reported relationships between peroxidasin expression and patient outcome in cancer.
Topics: Humans; Peroxidase; Extracellular Matrix Proteins; Collagen Type IV; Basement Membrane; Neoplasms; Tumor Microenvironment; Peroxidasin
PubMed: 37801286
DOI: 10.1042/BST20230018 -
Nature Communications May 2022Developing tunable and stable peroxidase mimetics with high catalytic efficiency provides a promising opportunity to improve and expand enzymatic catalysis in lignin...
Developing tunable and stable peroxidase mimetics with high catalytic efficiency provides a promising opportunity to improve and expand enzymatic catalysis in lignin depolymerization. A class of peptoid-based peroxidase mimetics with tunable catalytic activity and high stability is developed by constructing peptoids and hemins into self-assembled crystalline nanomaterials. By varying peptoid side chain chemistry to tailor the microenvironment of active sites, these self-assembled peptoid/hemin nanomaterials (Pep/hemin) exhibit highly modulable catalytic activities toward two lignin model substrates 2,2-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) and 3,3',5,5'-tetramethylbenzidine. Among them, a Pep/hemin complex containing the pyridyl side chain showed the best catalytic efficiency (V/K = 5.81 × 10 s). These Pep/hemin catalysts are highly stable; kinetics studies suggest that they follow a peroxidase-like mechanism. Moreover, they exhibit a high efficacy on depolymerization of a biorefinery lignin. Because Pep/hemin catalysts are highly robust and tunable, we expect that they offer tremendous opportunities for lignin valorization to high value products.
Topics: Biomimetics; Coloring Agents; Hemin; Lignin; Peptoids; Peroxidase; Peroxidases
PubMed: 35641490
DOI: 10.1038/s41467-022-30285-9 -
Journal of the American Society of... Nov 2018
Topics: Anti-Glomerular Basement Membrane Disease; Autoantigens; Extracellular Matrix Proteins; Glomerulonephritis; Humans; Peroxidase; Syndrome; Peroxidasin
PubMed: 30314979
DOI: 10.1681/ASN.2018090946 -
Biosensors Dec 2023Immunoassays based on antibodies as recognizing elements and enzymes as signal-generating modules are extensively used now in clinical lab diagnostics, food, and... (Review)
Review
Immunoassays based on antibodies as recognizing elements and enzymes as signal-generating modules are extensively used now in clinical lab diagnostics, food, and environmental analyses. However, the application of natural enzymes and antibodies has some drawbacks, such as relatively high manufacturing costs, thermal instability, and lot-to-lot variations that lower the reproducibility of results. Oligonucleotide aptamers are able to specifically bind their targets with high affinity and selectivity, so they represent a prospective alternative to protein antibodies for analyte recognition. Their main advantages include thermal stability and long shelf life, cost-efficient chemical synthesis, and negligible batch-to-batch variations. At the same time, a wide variety of non-protein peroxidase mimics are now available that show strong potential to replace protein enzymes. Here, we review and analyze non-protein biosensors that represent a nexus of these two concepts: aptamer-based sensors (aptasensors) with optical detection (colorimetric, luminescent, or fluorescent) based on different peroxidase mimics, such as DNAzymes, nanoparticles, or metal-organic frameworks.
Topics: Peroxidase; Prospective Studies; Reproducibility of Results; Peroxidases; Oligonucleotides; Biosensing Techniques; Antibodies; Aptamers, Nucleotide
PubMed: 38275302
DOI: 10.3390/bios14010001