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Relevant bibliographies by topics / Peroxygenase

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Academic literature on the topic 'Peroxygenase'

Author: Grafiati

Published: 4 June 2021

Last updated: 26 July 2025

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Journal articles on the topic "Peroxygenase"

1

Di, Siyu, Shengxian Fan, Fengjie Jiang, and Zhiqi Cong. "A Unique P450 Peroxygenase System Facilitated by a Dual-Functional Small Molecule: Concept, Application, and Perspective." Antioxidants 11, no. 3 (2022): 529. http://dx.doi.org/10.3390/antiox11030529.

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Cytochrome P450 monooxygenases (P450s) are promising versatile oxidative biocatalysts. However, the practical use of P450s in vitro is limited by their dependence on the co-enzyme NAD(P)H and the complex electron transport system. Using H2O2 simplifies the catalytic cycle of P450s; however, most P450s are inactive in the presence of H2O2. By mimicking the molecular structure and catalytic mechanism of natural peroxygenases and peroxidases, an artificial P450 peroxygenase system has been designed with the assistance of a dual-functional small molecule (DFSM). DFSMs, such as N-(ω-imidazolyl fatt

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Zámocký, Marcel, and Jana Harichová. "Evolution of Heme Peroxygenases: Ancient Roots and Later Evolved Branches." Antioxidants 11, no. 5 (2022): 1011. http://dx.doi.org/10.3390/antiox11051011.

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We reconstructed the molecular phylogeny of heme containing peroxygenases that are known as very versatile biocatalysts. These oxidoreductases capable of mainly oxyfunctionalizations constitute the peroxidase–peroxygenase superfamily. Our representative reconstruction revealed a high diversity but also well conserved sequence motifs within rather short protein molecules. Corresponding genes coding for heme thiolate peroxidases with peroxygenase activity were detected only among various lower eukaryotes. Most of them originate in the kingdom of fungi. However, it seems to be obvious that these

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3

Willot, Tieves, Girhard, Urlacher, Hollmann, and de Gonzalo. "P450BM3-Catalyzed Oxidations Employing Dual Functional Small Molecules." Catalysts 9, no. 7 (2019): 567. http://dx.doi.org/10.3390/catal9070567.

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A set of dual functional small molecules (DFSMs) containing different amino acids has been synthesized and employed together with three different variants of the cytochrome P450 monooxygenase P450BM3 from Bacillus megaterium in H2O2-dependent oxidation reactions. These DFSMs enhance P450BM3 activity with hydrogen peroxide as an oxidant, converting these enzymes into formal peroxygenases. This system has been employed for the catalytic epoxidation of styrene and in the sulfoxidation of thioanisole. Various P450BM3 variants have been evaluated in terms of activity and selectivity of the peroxyge

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4

Munro, Andrew W., Kirsty J. McLean, Job L. Grant, and Thomas M. Makris. "Structure and function of the cytochrome P450 peroxygenase enzymes." Biochemical Society Transactions 46, no. 1 (2018): 183–96. http://dx.doi.org/10.1042/bst20170218.

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The cytochromes P450 (P450s or CYPs) constitute a large heme enzyme superfamily, members of which catalyze the oxidative transformation of a wide range of organic substrates, and whose functions are crucial to xenobiotic metabolism and steroid transformation in humans and other organisms. The P450 peroxygenases are a subgroup of the P450s that have evolved in microbes to catalyze the oxidative metabolism of fatty acids, using hydrogen peroxide as an oxidant rather than NAD(P)H-driven redox partner systems typical of the vast majority of other characterized P450 enzymes. Early members of the pe

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5

Blée, Elizabeth. "Effect of the Safener Dichlormid on Maize Peroxygenase and Lipoxygenase." Zeitschrift für Naturforschung C 46, no. 9-10 (1991): 920–25. http://dx.doi.org/10.1515/znc-1991-9-1033.

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Abstract S-Ethyl-N,N-dipropylthiocarbamate (EPTC) was oxidized into its corresponding sulfoxide by microsomal fractions from etiolated maize seedlings. This reaction is catalyzed by a hydroperoxide-dependent enzyme, identified as a peroxygenase. The hydroperoxides formed from fatty acids by a lipoxygenase are efficient co-substrates of the EPTC sulfoxidation. The effects of the safener dichlormid on the peroxygenase and lipoxygenase activities were studied in vitro and in vivo. In vitro, the safener is not an inhibitor of these enzymes. Dichlormid seems to act, in vivo, by modulating the amoun

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6

Hofrichter, Martin, Harald Kellner, Robert Herzog, et al. "Peroxide-Mediated Oxygenation of Organic Compounds by Fungal Peroxygenases." Antioxidants 11, no. 1 (2022): 163. http://dx.doi.org/10.3390/antiox11010163.

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Unspecific peroxygenases (UPOs), whose sequences can be found in the genomes of thousands of filamentous fungi, many yeasts and certain fungus-like protists, are fascinating biocatalysts that transfer peroxide-borne oxygen (from H2O2 or R-OOH) with high efficiency to a wide range of organic substrates, including less or unactivated carbons and heteroatoms. A twice-proline-flanked cysteine (PCP motif) typically ligates the heme that forms the heart of the active site of UPOs and enables various types of relevant oxygenation reactions (hydroxylation, epoxidation, subsequent dealkylations, deacyl

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7

BLEE, ELIZABETH, and FRANCIS SCHUBER. "Properties of plant peroxygenase." Biochemical Society Transactions 20, no. 2 (1992): 223S. http://dx.doi.org/10.1042/bst020223s.

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8

Bassanini, Ivan, Erica Elisa Ferrandi, Marta Vanoni, et al. "Peroxygenase-Catalyzed Enantioselective Sulfoxidations." European Journal of Organic Chemistry 2017, no. 47 (2017): 7186–89. http://dx.doi.org/10.1002/ejoc.201701390.

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9

Carro, Juan, Elena Fernández-Fueyo, Carmen Fernández-Alonso, et al. "Self-sustained enzymatic cascade for the production of 2,5-furandicarboxylic acid from 5-methoxymethylfurfural." Biotechnology for Biofuels 11, no. 1 (2018): 86. https://doi.org/10.1186/s13068-018-1091-2.

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<strong>Background: </strong>2,5-Furandicarboxylic acid is a renewable building block for the production of polyfurandicarboxylates, which are biodegradable polyesters expected to substitute their classical counterparts derived from fossil resources. It may be produced from bio-based 5-hydroxymethylfurfural or 5-methoxymethylfurfural, both obtained by the acidic dehydration of biomass-derived fructose. 5-Methoxymethylfurfural, which is produced in the presence of methanol, generates less by-products and exhibits better storage stability than 5-hydroxymethylfurfural being, therefore, the indust

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Pesic, Milja, Sébastien Jean-Paul Willot, Elena Fernández-Fueyo, Florian Tieves, Miguel Alcalde, and Frank Hollmann. "Multienzymatic in situ hydrogen peroxide generation cascade for peroxygenase-catalysed oxyfunctionalisation reactions." Zeitschrift für Naturforschung C 74, no. 3-4 (2019): 101–4. http://dx.doi.org/10.1515/znc-2018-0137.

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Abstract There is an increasing interest in the application of peroxygenases in biocatalysis, because of their ability to catalyse the oxyfunctionalisation reaction in a stereoselective fashion and with high catalytic efficiencies, while using hydrogen peroxide or organic peroxides as oxidant. However, enzymes belonging to this class exhibit a very low stability in the presence of peroxides. With the aim of bypassing this fast and irreversible inactivation, we study the use of a gradual supply of hydrogen peroxide to maintain its concentration at stoichiometric levels. In this contribution, we

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Dissertations / Theses on the topic "Peroxygenase"

1

Cirino, Patrick Carmen Arnold Frances Hamilton. "Laboratory evolution of cytochrome P450 peroxygenase activity /." Diss., Pasadena, Calif. : California Institute of Technology, 2004. http://resolver.caltech.edu/CaltechETD:etd-06062003-164310.

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2

Ullrich, René, Martin Hofrichter, Marzena Poraj-Kobielska, et al. "Side chain removal from corticosteroids by unspecific peroxygenase." Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, 2018. http://nbn-resolving.de/urn:nbn:de:bsz:14-qucosa-235595.

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Two unspecific peroxygenases (UPO, EC 1.11.2.1) from the basidiomycetous fungi Marasmius rotula and Marasmius wettsteinii oxidized steroids with hydroxyacetyl and hydroxyl functionalities at C17 - such as cortisone, Reichstein's substance S and prednisone - via stepwise oxygenation and final fission of the side chain. The sequential oxidation started with the hydroxylation of the terminal carbon (C21) leading to a stable geminal alcohol (e.g. cortisone 21-gem-diol) and proceeded via a second oxygenation resulting in the corresponding α-ketocarboxylic acid (e.g. cortisone 21-oic acid). The lat

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Anari, Mohammad Reza. "Cytochrome P450 peroxidase/peroxygenase-dependent metabolic activation of xenobiotics." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1997. http://www.collectionscanada.ca/obj/s4/f2/dsk2/ftp03/NQ28269.pdf.

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Peter, Sebastian. "Oxyfunctionalization of alkanes, alkenes and alkynes by unspecific peroxygenase (EC 1.11.2.1)." Doctoral thesis, Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, 2013. http://nbn-resolving.de/urn:nbn:de:bsz:14-qucosa-113321.

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Unspecific peroxygenase (EC 1.11.2.1) represents a group of secreted hemethiolate proteins that are capable of catalyzing the selective mono-oxygenation of diverse organic compounds using only H2O2 as a cosubstrate. In this study, the peroxygenase from Agrocybe aegerita (AaeUPO) was found to catalyze the hydroxylation of various linear (e.g n-hexane), branched (e.g. 2,3-dimethylbutane) and cyclic alkanes (e.g. cyclohexane). The size of n-alkane substrates converted by AaeUPO ranged from gaseous propane (C3) to n-hexadecane (C16). They were mono-hydroxylated mainly at the C2 and C3 position, ra

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Barková, Kateřina. "Enzymatische Transformation verschiedener Flavonoide durch das extrazelluläre Pilzenzym Agrocybe-aegerita-Peroxygenase." Doctoral thesis, Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, 2013. http://nbn-resolving.de/urn:nbn:de:bsz:14-qucosa-124760.

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Die enzymatischen Transformationen mit der pilzlichen Peroxygenase aus Agrocybe aegerita haben gezeigt, dass das Enzym insgesamt über ein sehr breites Substratspektrum bezüglich der Flavonoide verfügt. Die Flavonoide werden mittels AaeAPO regioselektiv in 6-Position hydroxyliert. Der Reaktionsmechanismus der AaeAPO bei Flavonoiden läuft über eine Epoxidstufe ab, wobei der eingefügte Sauerstoff bei Hydroxylierungen dem Wasserstoffperoxid entstammt (Hinweis auf eine echte Peroxygenase-Reaktion). Die Enzymproduktion der Agrocybe aegerita wird durch den Extraktzusatz (aus jeweils Aronia melanocarp

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Kiebist, Jan, Kai-Uwe Schmidtke, Jörg Zimmermann, et al. "A peroxygenase from Chaetomium globosum catalyzes the selective oxygenation of testosterone." Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, 2017. http://nbn-resolving.de/urn:nbn:de:bsz:14-qucosa-222847.

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Unspecific peroxygenases (UPO, EC 1.11.2.1) secreted by fungi open an efficient way to selectively oxyfunctionalize diverse organic substrates, including less-activated hydrocarbons, by transferring peroxide-borne oxygen. We investigated a cell-free approach to incorporate epoxy and hydroxyl functionalities directly into the bulky molecule testosterone by a novel unspecific peroxygenase (UPO) that is produced by the ascomycetous fungus Chaetomium globosum in a complex medium rich in carbon and nitrogen. Purification by fast protein liquid chromatography revealed two enzyme fractions with the s

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Kinne, Matthias. "The extracellular peroxygenase of the agaric fungus Agrocybe aegerita: catalytic properties and physiological background with particular emphasis on ether cleavage." Doctoral thesis, Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, 2010. http://nbn-resolving.de/urn:nbn:de:bsz:14-qucosa-62076.

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Litter-decay fungi have recently been shown to secrete heme-thiolate peroxygenases that oxidize various organic chemicals, but little is known about the physiological role or the mechanism of these enzymes. The aromatic peroxygenase of Agrocybe aegerita (AaeAPO) was purified and catalytically characterized. An overall reaction mechanism was proposed. The results show that AaeAPO catalyzed diverse H2O2-dependent monooxygenations (two-electron oxidations) including (a) the cleavage of aliphatic and aromatic ethers, (b) the regio- and enantioselective hydroxylation of aromatic compounds, (c) the

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8

Fuchs, Christopher [Verfasser], Wilfried [Akademischer Betreuer] Schwab, and Karl-Heinz [Akademischer Betreuer] Engel. "Funktionalisierung von Lipiden durch Peroxygenase / Christopher Fuchs. Gutachter: Karl-Heinz Engel ; Wilfried Schwab. Betreuer: Wilfried Schwab." München : Universitätsbibliothek der TU München, 2013. http://d-nb.info/1038527139/34.

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9

COCCO, GIANMARCO. "Biomimetic emulators of high potential peroxygenases: Implications in bioremediation and metabolic studies." Doctoral thesis, Università degli Studi di Cagliari, 2016. http://hdl.handle.net/11584/266700.

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Nowadays, classical (bio)remediation processes are affected by some economical and environmental drawbacks. These approaches often seem to be inadequate, particularly in the perspective of sustainable green processes. Since immobilized metalloporphines can emulate the active site of peroxidases and peroxygenases, their use in several bioremediation processes has been analyzed in this work. The described catalytic reactions use bioinspired, homogenized or heterogenized, commercial porphines and showed a remarkable ability to catalyze substrates oxidation at the expenses of different oxidants su

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10

Shersher, Elena. "The Influence of the Proximal Thiolate Ligand and Hydrogen Bond Network of the Proximal Helix on the Structural and Biochemical Properties of Chloroperoxidase." FIU Digital Commons, 2016. http://digitalcommons.fiu.edu/etd/2483.

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Chloroperoxidase (CPO) from Caldariomyces fumago is a versatile heme enzyme with great potential for environmental and pharmaceutical applications. It catalyzes a plethora of reactions including halogenation, dismutation, epoxidation, and oxidation. The diverse catalytic capabilities of CPO have long been attributed to the protein’s distinct active site that combines structural features of peroxidases and cytochromes P450. Particularly, the role of the axial thiolate ligand in CPO catalysis has been much debated. Furthermore, no data are available on the role of hydrogen bonding between Arg 26

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Books on the topic "Peroxygenase"

1

Hrycay, Eugene G., and Stelvio M. Bandiera, eds. Monooxygenase, Peroxidase and Peroxygenase Properties and Mechanisms of Cytochrome P450. Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-16009-2.

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Wang, Xiaoshi. A Novel Heme-Thiolate Peroxygenase AaeAPO and Its Implications for C-H Activation Chemistry. Springer International Publishing, 2016. http://dx.doi.org/10.1007/978-3-319-03236-8.

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3

Anari, Mohammad Reza. Cytochrome P450 peroxidase/peroxygenase-dependent metabolic activation of xenobiotics. 1997.

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Hrycay, Eugene G., and Stelvio M. Bandiera. Monooxygenase, Peroxidase and Peroxygenase Properties and Mechanisms of Cytochrome P450. Springer, 2015.

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Hrycay, Eugene G., and Stelvio M. Bandiera. Monooxygenase, Peroxidase and Peroxygenase Properties and Mechanisms of Cytochrome P450. Springer International Publishing AG, 2016.

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Hrycay, Eugene G., and Stelvio M. Bandiera. Monooxygenase, Peroxidase and Peroxygenase Properties and Mechanisms of Cytochrome P450. Springer, 2015.

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Wang, Xiaoshi. Novel Heme-Thiolate Peroxygenase AaeAPO and Its Implications for C-H Activation Chemistry. Springer International Publishing AG, 2015.

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Wang, Xiaoshi. Novel Heme-Thiolate Peroxygenase AaeAPO and Its Implications for C-H Activation Chemistry. Springer International Publishing AG, 2016.

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Wang, Xiaoshi. Novel Heme-Thiolate Peroxygenase AaeAPO and Its Implications for C-H Activation Chemistry. Springer, 2015.

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Book chapters on the topic "Peroxygenase"

1

Schomburg, Dietmar, and Ida Schomburg. "unspecific peroxygenase 1.11.2.1." In Class 1 Oxidoreductases. Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-36265-1_66.

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Molina-Espeja, Patricia, Patricia Gómez de Santos, and Miguel Alcalde. "Directed Evolution of Unspecific Peroxygenase." In Directed Enzyme Evolution: Advances and Applications. Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-50413-1_5.

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3

Blée, Elizabeth, and Francis Schuber. "Oxylipins in Plants: The Peroxygenase Pathway." In Plant Lipid Metabolism. Springer Netherlands, 1995. http://dx.doi.org/10.1007/978-94-015-8394-7_72.

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Yarman, Aysu, Lei Peng, Yunhua Wu, et al. "Can peroxygenase and microperoxidase substitute cytochrome P450 in biosensors." In Frontiers of Bioanalytical Chemistry. Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-36303-0_10.

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Wang, Xiaoshi. "Detection and Characterization of Heme-Thiolate Compound II from AaeAPO Peroxygenase." In A Novel Heme-Thiolate Peroxygenase AaeAPO and Its Implications for C-H Activation Chemistry. Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-03236-8_6.

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Wang, Xiaoshi. "Efficient and Selective Alkane Hydroxylation Reactions Catalyzed by the Fungal Peroxygenase AaeAPO." In A Novel Heme-Thiolate Peroxygenase AaeAPO and Its Implications for C-H Activation Chemistry. Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-03236-8_2.

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Hrycay, Eugene G., and Stelvio M. Bandiera. "Monooxygenase, Peroxidase and Peroxygenase Properties and Reaction Mechanisms of Cytochrome P450 Enzymes." In Advances in Experimental Medicine and Biology. Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-16009-2_1.

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Wang, Xiaoshi. "Detection and Kinetic Characterization of a Highly Reactive Heme-Thiolate Peroxygenase AaeAPO Compound I." In A Novel Heme-Thiolate Peroxygenase AaeAPO and Its Implications for C-H Activation Chemistry. Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-03236-8_4.

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Wang, Xiaoshi. "Hydrocarbon Oxygenation by Heme-Thiolate Enzymes." In A Novel Heme-Thiolate Peroxygenase AaeAPO and Its Implications for C-H Activation Chemistry. Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-03236-8_1.

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Wang, Xiaoshi. "Hydrocarbon Hydroxylations Catalyzed by AaeAPO: Evidence of Radical Intermediates and Kinetic Isotope Effects." In A Novel Heme-Thiolate Peroxygenase AaeAPO and Its Implications for C-H Activation Chemistry. Springer International Publishing, 2015. http://dx.doi.org/10.1007/978-3-319-03236-8_3.

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