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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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3

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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4

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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5

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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6

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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7

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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11

Kwong, Lam Elwood. "Investigating the Role of the Proximal Cysteine Hydrogen Bonding Network and Distal Pocket in Chloroperoxidase." FIU Digital Commons, 2018. https://digitalcommons.fiu.edu/etd/3898.

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Chloroperoxidase (CPO) is one of the most versatile heme enzyme isolated from the marine fungus, Caldariomyces fumago. Functionally, CPO can catalyze four types of reactions: peroxidation (peroxidase-like), dismutation (catalase-like), halogenation (halogenase-like), and peroxygenation (P450-like). Structurally, CPO has a distal and proximal pockets that can be best described as a hybrid of classical peroxidase and P450s. As a heme-thiolate protein, CPO contains the conserved proximal Pro28-Cys29-Pro30 stretch found in other members of the family. However, the structural and functional roles o
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12

Peter, Sebastian [Verfasser], Martin [Akademischer Betreuer] Hofrichter, John T. [Akademischer Betreuer] Groves, and Katrin [Akademischer Betreuer] Scheibner. "Oxyfunctionalization of alkanes, alkenes and alkynes by unspecific peroxygenase (EC 1.11.2.1) / Sebastian Peter. Gutachter: Martin Hofrichter ; John T. Groves ; Katrin Scheibner. Betreuer: Martin Hofrichter." Dresden : Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, 2013. http://d-nb.info/1068152370/34.

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13

Pecyna, Marek. "Molekularbiologische Charakterisierung von Häm-Thiolat- und DyP-type-Peroxidasen ausgewählter Basidiomyceten." Doctoral thesis, Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, 2016. http://nbn-resolving.de/urn:nbn:de:bsz:14-qucosa-209428.

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Peroxidasen des Typs ClassII sowie die Chlorperoxidase waren für mehrere Jahrzehnte die einzigen bekannten sekretorischen Hämperoxidasen aus Pilzen. Im Jahr 2004 wurde eine neue, ungewöhnliche Hämperoxidase aus dem Speisepilz Agrocybe aegerita isoliert und biochemisch charakterisiert. Diese Peroxidase, heute offiziell Unspezifische Peroxygenase (UPO, EC 1.11.2.1) genannt, vereint in sich Eigenschaften sowohl intrazellulärer Cytochrom-P450-Enzyme als auch klassischer extrazellulärer, pilzlicher Peroxidasen des Typs ClassII. In dieser Arbeit wurden für den UPO-Modellorganismus A. aegerita und fü
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14

Barková, Kateřina [Verfasser], Martin [Akademischer Betreuer] Hofrichter, Annett [Akademischer Betreuer] Fuchs, and Frieder [Akademischer Betreuer] Schauer. "Enzymatische Transformation verschiedener Flavonoide durch das extrazelluläre Pilzenzym Agrocybe-aegerita-Peroxygenase / Kateřina Barková. Gutachter: Martin Hofrichter ; Annett Fuchs ; Frieder Schauer. Betreuer: Martin Hofrichter ; Annett Fuchs." Dresden : Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, 2013. http://d-nb.info/1068154055/34.

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15

Karich, Alexander, Sebastian B. Kleeberg, René Ullrich, and Martin Hofrichter. "Enzymatic Preparation of 2,5-Furandicarboxylic Acid (FDCA)—A Substitute of Terephthalic Acid—By the Joined Action of Three Fungal Enzymes." Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, 2018. http://nbn-resolving.de/urn:nbn:de:bsz:14-qucosa-234705.

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Enzymatic oxidation of 5-hydroxymethylfurfural (HMF) and its oxidized derivatives was studied using three fungal enzymes: wild-type aryl alcohol oxidase (AAO) from three fungal species, wild-type peroxygenase from Agrocybe aegerita (AaeUPO), and recombinant galactose oxidase (GAO). The effect of pH on different reaction steps was evaluated and apparent kinetic data (Michaelis-Menten constants, turnover numbers, specific constants) were calculated for different enzyme-substrate ratios and enzyme combinations. Finally, the target product, 2,5-furandicarboxylic acid (FDCA), was prepared in a mult
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16

Poraj-Kobielska, Marzena. "Conversion of pharmaceuticals and other drugs by fungal peroxygenases." Doctoral thesis, Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, 2013. http://nbn-resolving.de/urn:nbn:de:bsz:14-qucosa-113339.

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Over the recent years, increasing scientific attention has been paid to pharmaceuticals, other drugs and their metabolites. These substances are of particular interest because of their physiological, toxicological and ecotoxicological effects in the human body and respectively in the environment. Cytochrome P450 enzymes (P450s) play a key role in the conversion and detoxification of bioactive compounds including many pharmaceuticals and drugs. Most of these enzymes belong to the monooxygenases; they are intracellular and rather unstable biocatalysts that are difficult to purify and require exp
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17

Mielke, Tamara. "Heterologous expression and characterisation of unspecific peroxygenases." Thesis, University of York, 2016. http://etheses.whiterose.ac.uk/20015/.

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In 2004, unspecific peroxygenases (UPOs) from fungi were first identified and showed to catalyse selective oxygenation reactions, with high turnovers, good stability and a broad reaction scope, providing a valuable alternative to established biocatalytic hydroxylation systems such as cytochrome P450s. At the start of this project, access to UPOs was limited to expression in their native fungi, hence studies were performed looking into heterologous expression of the enzymes from Agrocybe aegerita and Agaricus bisporus, followed by characterisation, and application of the enzymes.
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18

Auty, Kevin. "Peroxygens in catalysed aromatic side-chain oxidations." Thesis, University of York, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.337658.

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19

Matthews, Sarah. "Characterisation and engineering of alkene producing P450 peroxygenases for bioenergy applications." Thesis, University of Manchester, 2017. https://www.research.manchester.ac.uk/portal/en/theses/characterisation-and-engineering-of-alkene-producing-p450-peroxygenases-for-bioenergy-applications(2d1b8751-2be3-48ab-8b4e-d1844ffc690d).html.

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OleTJE (CYP152L1) is a P450 peroxygenase that was first isolated from Jeotgalicoccus sp. 8456 in 2011. OleTJE is primarily a fatty acid decarboxylase, converting mid-chain fatty acids (C10:0 to C22:0) to terminal alkenes, which are industrially useful petrochemicals. Terminal alkenes are hydrophobic with high energy density, and are compatible with existing transportation infrastructure. Thus OleTJE has attracted considerable interest due to potential applications for generating "drop-in" biofuels. As a P450 peroxygenase, OleTJE is able to utilise H2O2 as a sole oxygen and hydrogen donor. This
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20

Watts, Simon Francis. "The acid leaching of uranium dioxide with peroxygens." Thesis, Imperial College London, 1986. http://hdl.handle.net/10044/1/38182.

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21

Karich, Alexander [Verfasser], Martin [Gutachter] Hofrichter, and Frank [Gutachter] Hollmann. "Performance pilzlicher Peroxygenasen in einfachen und kaskadischen Oxyfunktionalisierungsreaktionen / Alexander Karich ; Gutachter: Martin Hofrichter, Frank Hollmann." Dresden : Technische Universität Dresden, 2020. http://d-nb.info/1227312814/34.

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22

Kimani, Virginia Wambui [Verfasser], Martin [Gutachter] Hofrichter, and Richard P. [Gutachter] Beckett. "New Secretory Peroxidases and Peroxygenases from Saprotrophic Fungi of Kenyan Forests / Virginia Wambui Kimani ; Gutachter: Martin Hofrichter, Richard P. Beckett." Dresden : Technische Universität Dresden, 2020. http://d-nb.info/1227053835/34.

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23

Poraj-Kobielska, Marzena [Verfasser], Martin [Akademischer Betreuer] Hofrichter, Kenneth E. [Akademischer Betreuer] Hammel, and Korneliusz [Akademischer Betreuer] Miksch. "Conversion of pharmaceuticals and other drugs by fungal peroxygenases / Marzena Poraj-Kobielska. Gutachter: Martin Hofrichter ; Kenneth E. Hammel ; Korneliusz Miksch. Betreuer: Martin Hofrichter." Dresden : Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, 2013. http://d-nb.info/1068152397/34.

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24

LEROUX-OFFNER, VALERIE. "Destruction chimique d'ester organophosphore en milieu micellaire par les nucleophiles alpha peroxygenes : efficacite relative de peracide, de perborate et de l'anion perhydroxyle. etude cinetique et echange d'anions a l'interface micellaire." Paris 7, 1995. http://www.theses.fr/1995PA077130.

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Les vitesses de coupure esterolytique du p-nitrophenyldiphenylphosphate, pris comme modele de compose organophosphore, par differents nucleophiles alpha peroxygenes ont ete mesurees a un ph voisin de 9 en milieu micellaire avec l'acetate de cetyltrimethylammonium comme tensioactif. Des temps de demi-reaction tres courts ont ainsi ete obtenus avec l'anion perhydroxyle (20s), le perborate (5s) et le monoperphtalate de magnesium, mmpp, (0,2s). L'analyse des effets cinetiques des concentrations du tensioactif et du nucleophile a ete realisee en adaptant le modele de pseudophase et d'echange d'ions
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25

Cirino, Patrick Carmen. "Laboratory Evolution of Cytochrome P450 Peroxygenase Activity." Thesis, 2004. https://thesis.library.caltech.edu/2469/2/cirinothesis.pdf.

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<p>The ability of the cytochrome P450 heme monooxygenases to catalyze difficult oxidation reactions, often with high specificity and selectivity, makes them attractive for numerous biotechnological applications. However they are generally limited by low turnover rates and low stability, and their minimum requirements for catalysis include a cofactor as source of electrons (NAD(P)H), partner proteins for electron transfer, and dioxygen. Some P450s are capable of supporting low levels of peroxygenase activity, in which a peroxide is utilized to drive catalysis via a "shunt" pathway. This mech
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26

Peter, Sebastian. "Oxyfunctionalization of alkanes, alkenes and alkynes by unspecific peroxygenase (EC 1.11.2.1): Oxyfunctionalization of alkanes, alkenes and alkynes by unspecific peroxygenase (EC 1.11.2.1)." Doctoral thesis, 2012. https://tud.qucosa.de/id/qucosa%3A26900.

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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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27

Barková, Kateřina. "Enzymatische Transformation verschiedener Flavonoide durch das extrazelluläre Pilzenzym Agrocybe-aegerita-Peroxygenase." Doctoral thesis, 2012. https://tud.qucosa.de/id/qucosa%3A27198.

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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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28

"MOLECULAR ANALYSIS OF FATTY ACID PEROXYGENASE INVOLVED IN THE BIOSYNTHESIS OF EPOXY FATTY ACIDS IN OATS (Avena sativa)." Thesis, 2015. http://hdl.handle.net/10388/ETD-2015-10-2275.

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Oat is known to synthesize several epoxy fatty acids in seeds using peroxygenase (PXG), a type of hydroperoxide-dependent epoxygenase. This thesis aims to molecularly clone and functionally characterize the PXG genes from oat developing seeds. The research started with identifying additional PXG genes from oat expressed sequence tag (EST) databases using a previously identified oat peroxygenase AsPXG1 as a query sequence. This resulted in the identification of six homologous contig sequences from the EST data bases. Of them, two contigs with high sequence similarity and alignment with plant PX
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29

Karich, Alexander. "Performance pilzlicher Peroxygenasen in einfachen und kaskadischen Oxyfunktionalisierungsreaktionen." 2020. https://tud.qucosa.de/id/qucosa%3A73100.

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Die vorliegende Arbeit befasst sich mit der unspezifischen Peroxygenase (UPO), einer ausschließlich von Pilzen produzierten Oxidoreduktase. Die Dissertation besteht aus drei wesentlichen Teilen: 1.) Untersuchungen zum Substratspektrum zweier ausgewählter UPOs, 2.) Untersuchungen zur Inaktivierung von UPOs, und 3.) die Etablierung einer Kaskadenreaktion von UPOs und pilzlichen Oxidasen zur Oxidation von Hydroxymethylfurfural (HMF) zu 2,5-Furandicarbonsäure (FDCA). 1) Oxidation ausgewählter organischer Schadstoffe Die Mehrheit der getesteten organischen Schadstoffe (35 von 44 chemischen Verbin
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30

Kinne, Matthias [Verfasser]. "The extracellular peroxygenase of the agaric fungus Agrocybe aegerita: catalytic properties and physiological background with particular emphasis on ether cleavage = Die extrazelluläre Peroxygenase des Lammellenpilzes Agrocybe aegerita: katalytische Eigenschaften und physiologischer Hintergrund unter besonderer Berücksichtigung der Etherspaltung / von Matthias Kinne." 2010. http://d-nb.info/1010396323/34.

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31

Podgorski, Matthew Nathanial. "Investigation of the Mechanism of Multiple Cytochrome P450-catalysed Reactions." Thesis, 2019. http://hdl.handle.net/2440/123404.

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The cytochrome P450 heme-thiolate enzymes catalyse a multitude of oxidation reactions and, in humans, carry out drug metabolism. P450s perform hydroxylation, epoxidation, N-, O- and Sdealkylation, sulfoxidation, alkyne oxidation and aldehyde oxidation of organic molecules (and many other reactions). These reactions are predominantly performed by the reactive intermediate Compound I, but other intermediates in the catalytic cycle may mediate some types of reactions. It would be appealing to exploit these enzymes as environmentally benign catalysts in the synthesis of fine chemicals. Their wides
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32

Kimani, Virginia Wambui. "New Secretory Peroxidases and Peroxygenases from Saprotrophic Fungi of Kenyan Forests." 2019. https://tud.qucosa.de/id/qucosa%3A38041.

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Die vorliegende Dissertation befasst sich vor dem Hintergrund von pilzlicher Ökophysiologie und Umweltbiotechnologie mit der Isolierung, Reinigung und Charakterisierung von neuartigen Oxidoreduktasen aus kenianischen Pilzen (Eumycota). Unter Verwendung von selektiven, antibiotikahaltigen Agarmedien wurde 2016 eine Stammsammlung von 43 pilzlichen Isolaten angelegt, die Totholz, Laubstreu und Boden besiedelnde Arten umfasst und drei verschiedene kenianische Waldtypen und Biodiversitätsschwerpunkte berücksichtigt (ostafrikanische Regen-, Berg- und Küstenwälder). Die Isolate gehörten zu 21 Familie
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33

Pecyna, Marek. "Molekularbiologische Charakterisierung von Häm-Thiolat- und DyP-type-Peroxidasen ausgewählter Basidiomyceten." Doctoral thesis, 2015. https://tud.qucosa.de/id/qucosa%3A29761.

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Peroxidasen des Typs ClassII sowie die Chlorperoxidase waren für mehrere Jahrzehnte die einzigen bekannten sekretorischen Hämperoxidasen aus Pilzen. Im Jahr 2004 wurde eine neue, ungewöhnliche Hämperoxidase aus dem Speisepilz Agrocybe aegerita isoliert und biochemisch charakterisiert. Diese Peroxidase, heute offiziell Unspezifische Peroxygenase (UPO, EC 1.11.2.1) genannt, vereint in sich Eigenschaften sowohl intrazellulärer Cytochrom-P450-Enzyme als auch klassischer extrazellulärer, pilzlicher Peroxidasen des Typs ClassII. In dieser Arbeit wurden für den UPO-Modellorganismus A. aegerita und fü
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34

Poraj-Kobielska, Marzena. "Conversion of pharmaceuticals and other drugs by fungal peroxygenases." Doctoral thesis, 2012. https://tud.qucosa.de/id/qucosa%3A26901.

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Over the recent years, increasing scientific attention has been paid to pharmaceuticals, other drugs and their metabolites. These substances are of particular interest because of their physiological, toxicological and ecotoxicological effects in the human body and respectively in the environment. Cytochrome P450 enzymes (P450s) play a key role in the conversion and detoxification of bioactive compounds including many pharmaceuticals and drugs. Most of these enzymes belong to the monooxygenases; they are intracellular and rather unstable biocatalysts that are difficult to purify and require exp
APA, Harvard, Vancouver, ISO, and other styles
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