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1

Tatzel, Stephan. "Modellierung von Cytochrom P450-Monooxygenasen." [S.l. : s.n.], 2008. http://nbn-resolving.de/urn:nbn:de:bsz:93-opus-34577.

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2

Leipold, Friedemann [Verfasser]. "Untersuchungen zu rekombinanten eukaryotischen Baeyer-Villiger-Monooxygenasen / Friedemann Leipold." Greifswald : Universitätsbibliothek Greifswald, 2013. http://d-nb.info/1033281859/34.

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3

Thönnessen, Alexandra [Verfasser]. "Funktionelle Charakterisierung von flavinhaltigen Monooxygenasen in Arabidopsis thaliana / Alexandra Thönnessen." Aachen : Hochschulbibliothek der Rheinisch-Westfälischen Technischen Hochschule Aachen, 2012. http://d-nb.info/1022868403/34.

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4

Born, Ariane. "Etablierung und Optimierung der Error-Prone-PCR und eines Aktivitätsscreenings für Styrol-Monooxygenasen." Master's thesis, Technische Universitaet Bergakademie Freiberg Universitaetsbibliothek "Georgius Agricola", 2011. http://nbn-resolving.de/urn:nbn:de:bsz:105-qucosa-77143.

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Styrol-Monooxygenasen (SMOs) spielen im bakteriellen Abbau von Styrol eine wichtige Rolle. Sie epoxidieren den Kohlenwasserstoff zu (S)-Styroloxid und waren bis vor kurzem vor allem aus Gram-negativen Vertretern wie Pseudomonaden bekannt. Das Grampositive nocardioforme Bodenbakterium Rhodococcus opacus 1CP kann Styrol als Energie- und Kohlenstoffquelle nutzen und verfügt über zwei Typen von SMOs. Neben StyA2B, einer fusionierten FAD:NADH-Oxidoreduktase (StyB) und Monooxygenase (StyA2) findet sich eine weitere Monooxygenase StyA1, deren Gen direkt stromaufwärts zu styA2B lokalisiert ist. Zusätz
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5

Sehlmeyer, Sven [Verfasser], and Dietrich [Akademischer Betreuer] Ober. "Flavin-abhängige Monooxygenasen aus N-oxygenierenden Arctiiden / Sven Sehlmeyer ; Betreuer: Dietrich Ober." Braunschweig : Technische Universität Braunschweig, 2010. http://d-nb.info/1175828041/34.

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6

Budde, Michael. "Biokatalyse mit Cytochrom P450 Monooxygenasen: zur selektiven Oxidation von Terpenen und Fettsäuren." [S.l. : s.n.], 2007. http://nbn-resolving.de/urn:nbn:de:bsz:93-opus-32363.

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7

Wimalasena, Kandatege. "Mechanistic studies on non-heme monooxygenases : dopamine [beta]-monooxygenase and pseudomonas oleovorans monooxygenase system." Diss., Georgia Institute of Technology, 1986. http://hdl.handle.net/1853/27070.

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8

Ullmann, Christoph. "Untersuchungen zur Wirkung von Propiverin auf spezifische Cytochrom-P450-abhängige Monooxygenasen in der Rattenleber." [S.l.] : [s.n.], 2000. http://web.ub.uni-greifswald.de/eDiss/2001/2.

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9

Erber, Astrid Maria [Verfasser], and Andreas [Akademischer Betreuer] Bechthold. "Untersuchungen zu Luciferase-ähnlichen Monooxygenasen, Flavinreduktasen und Ketoreduktasen aus dem Mensacarcin-Produzenten Streptomyces bottropensis." Freiburg : Universität, 2017. http://d-nb.info/1135572178/34.

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10

Lutz-Wahl, Sabine. "Selektive Hydroxylierung von Alpha- und Beta-Ionon durch Streptomyces-Stämme und molekulargenetische Arbeiten zur Identifizierung und Isolierung der Ionon-Hydroxylase aus Streptomyces fradiae Tü 27 /." [S.l. : s.n.], 1999. http://www.bsz-bw.de/cgi-bin/xvms.cgi?SWB8339140.

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11

Wang, Linzhu [Verfasser]. "Molekulare Identifizierung und Charakterisierung der Flavin-abhängigen Monooxygenasen in verschiedenen Pyrrolizidin-Alkaloid-adaptierten Insekten / Linzhu Wang." Kiel : Universitätsbibliothek Kiel, 2013. http://d-nb.info/1031190201/34.

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12

Specker, Silvia. "Klonierung von Cytochrom-P450-abhängigen Monooxygenasen aus Ammi majus L. und funktionelle Expression der Zimtsäure 4-Hydroxylase." [S.l. : s.n.], 2004. http://archiv.ub.uni-marburg.de/diss/z2004/0072/.

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13

Kranz-Finger, Sarah [Verfasser], Vlada B. [Gutachter] Urlacher, and Karl-Erich [Gutachter] Jaeger. "Oxidation pflanzlicher Triterpenoide mittels Cytochrom-P450-Monooxygenasen / Sarah Kranz-Finger ; Gutachter: Vlada B. Urlacher, Karl-Erich Jaeger." Düsseldorf : Universitäts- und Landesbibliothek der Heinrich-Heine-Universität Düsseldorf, 2019. http://d-nb.info/1196870691/34.

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14

Kranz-Finger, Sarah Katharina [Verfasser], Vlada B. [Gutachter] Urlacher, and Karl-Erich [Gutachter] Jaeger. "Oxidation pflanzlicher Triterpenoide mittels Cytochrom-P450-Monooxygenasen / Sarah Kranz-Finger ; Gutachter: Vlada B. Urlacher, Karl-Erich Jaeger." Düsseldorf : Universitäts- und Landesbibliothek der Heinrich-Heine-Universität Düsseldorf, 2019. http://d-nb.info/1196870691/34.

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15

Pisch-Heberle, Sandra. "Untersuchungen zur Stabilisierung von Membranproteinen mit ungewöhnlichen Phospholipiden." [S.l.] : Universität Stuttgart , Fakultät Chemie , Institut für Technische Biochemie, 2000. http://www.bsz-bw.de/cgi-bin/xvms.cgi?SWB8619088.

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16

Weber, Evelyne [Verfasser], and Bernhard [Akademischer Betreuer] Hauer. "Protein Engineering von P450-Monooxygenasen zur selektiven Hydroxylierung von cyclischen und acyclischen Alkanen / Evelyne Weber. Betreuer: Bernhard Hauer." Stuttgart : Universitätsbibliothek der Universität Stuttgart, 2011. http://d-nb.info/1017588333/34.

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17

Rühlmann, Ansgar [Verfasser], Vlada B. [Akademischer Betreuer] Urlacher, and Georg [Akademischer Betreuer] Groth. "Charakterisierung und Proteinengineering von P450-Monooxygenasen der CYP154-Familie für die Biokatalyse / Ansgar Rühlmann ; Vlada B. Urlacher, Georg Groth." Düsseldorf : Universitäts- und Landesbibliothek der Heinrich-Heine-Universität Düsseldorf, 2017. http://d-nb.info/1139491156/34.

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18

Rabe, Volker. "Neue Nicht-Häm-Eisenkomplexe Synthese, spektroskopische Charakterisierung und Anwendung in der katalytischen aeroben C-H-Oxidation." Berlin mbv, Mensch-und-Buch-Verl, 2009. http://d-nb.info/1000289982/04.

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19

Rimmel, Nina [Verfasser], Volker [Akademischer Betreuer] [Gutachter] Sieber та Wilfried [Gutachter] Schwab. "Selektive ω-Oxidation aliphatischer Substrate – Charakterisierung von Monooxygenasen und Etablierung einer Biotransformationsplattform / Nina Rimmel ; Gutachter: Volker Sieber, Wilfried Schwab ; Betreuer: Volker Sieber". München : Universitätsbibliothek der TU München, 2016. http://d-nb.info/1120013674/34.

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20

Ruff, Anna Joëlle [Verfasser]. "Advances in directed monooxygenase evolution : from diversity generation and flow cytometry screening to tailor-made monooxygenases / Anna Joëlle Ruff." Aachen : Hochschulbibliothek der Rheinisch-Westfälischen Technischen Hochschule Aachen, 2013. http://d-nb.info/1031116346/34.

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21

Xie, Weihong. "Bioelectrochemistry of monooxygenases." Thesis, University of Oxford, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.343062.

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22

Beecher, Jean Elizabeth. "Sulfoxidation by microbial monooxygenases." Thesis, University of Exeter, 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.244958.

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23

Colbert, James Early Jr. "Mechanistic and biotechnological investigations of pseudomonas oleovorans monooxygenase and enantiospecificity of dopamine B-monooxygenase." Diss., Georgia Institute of Technology, 1989. http://hdl.handle.net/1853/27862.

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24

Schneider, Toni. "Gerichtete Evolution als Methode zur Erzeugung enantioselektiver Cyclohexanonmonooxygenasen (CHMOs) für die Katalyse von Baeyer-Villiger-Reaktionen." [S.l.] : [s.n.], 2005. http://deposit.ddb.de/cgi-bin/dokserv?idn=97392358X.

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25

Bhambra, Amarbalita. "The regulatory protein of methane monooxygenase." Thesis, University of Warwick, 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.319794.

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26

Balendra, Suki. "Component interactions of soluble methane monooxygenase." Thesis, University of Warwick, 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.250111.

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27

Carnell, Andrew John. "Cycloalkanone monooxygenase enzymes in organic synthesis." Thesis, University of Exeter, 1991. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.293971.

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28

Milne, Gavin D. S. "Inhibition studies of kynurenine 3-monooxygenase." Thesis, University of St Andrews, 2013. http://hdl.handle.net/10023/4101.

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Kynurenine 3-monooxygenase (K3MO) lies on the kynurenine pathway, the major pathway for the catabolism of L-tryptophan. It converts kynurenine to 3-hydroxy kynurenine. Inhibition of K3MO is important in several neurological diseases and there is evidence that inhibition of K3MO could also be targeted for the prevention of multiple organ failure, secondary to acute pancreatitis. A structure activity relationship based upon the 1,2,4-oxadiazoles motif was carried out which revealed amide 207 as an inhibitor of P. fluorescens K3MO. Further structure activity relationships were developed based upo
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29

Thevandavakkam, Mathuravani Aaditiyaa. "Deciphering the kynurenine-3-monooxygenase interactome." Thesis, University of Leicester, 2011. http://hdl.handle.net/2381/10070.

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Kynurenine-3-monooxygenase (KMO) is a mitochondrial enzyme in the kynurenine pathway (KP) through which tryptophan is degraded to NAD+. The central KP is altered in neurodegenerative diseases and other CNS disorders. The causative role of KP metabolites has been particularly well studied in the neurodegenerative disorder Huntington’s disease (HD), a fatal adult onset condition inherited in an autosomal dominant manner. In HD, flux in the KP is perturbed such that neurotoxic metabolites (3-hydroxykynurenine and quinolinic acid) of the pathway are increased relative to a neuroprotective metaboli
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30

Tinberg, Christine Elaine. "Exploring the reactivity of bacterial multicomponent monooxygenases." Thesis, Massachusetts Institute of Technology, 2010. http://hdl.handle.net/1721.1/62059.

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Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Chemistry, 2010.<br>Vita. Cataloged from PDF version of thesis.<br>Includes bibliographical references.<br>Chapter 1. Introduction: The Reactivity of Bacterial Multicomponent Monooxygenases Bacterial multicomponent monooxygenases constitute a remarkable family of enzymes that oxidize small, inert hydrocarbon substrates using molecular oxygen. Three or more protein components are required for the timely reactions of electrons, protons, 02, and hydrocarbon at an active site carboxylate-bridged diiron center. This overview describes
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31

Kaelin, A. C. "A characterization of human placental monooxygenase activity." Thesis, Brunel University, 1986. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.374837.

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32

Gonzalez, Malagon S. G. "Flavin containing monooxygenase 5 and endogenous metabolism." Thesis, University College London (University of London), 2012. http://discovery.ucl.ac.uk/1338406/.

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To gain insights into the endogenous role of flavin-containing monooxygenase 5 (FMO5), the phenotype of male Fmo5 knockout mice was investigated. Up to 22 weeks of age Fmo5 -/- male mice have a similar body weight to wild-type animals. However, from 30-weeks of age the knockout mice have a reduced weight gain. Gonadal fat deposits are smaller in young (4-week old), but are greatly reduced in older knockout animals. Despite the lower body weight and reduced fat deposits, the older Fmo5 -/- mice show increased food intake. They do not exhibit increased activity but have an increased metabolic ra
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33

Avenell, Philip James. "Downstream processing from Baeyer-Villiger monooxygenase bioconversions." Thesis, University College London (University of London), 2003. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.404921.

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34

Shears, J. H. "Studies on ammonia monooxygenase of Nitrosomonas europaea." Thesis, University of Bristol, 1986. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.373853.

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35

Feng, Xudong. "Structural and functional models for methane monooxygenase." Thesis, Massachusetts Institute of Technology, 1991. http://hdl.handle.net/1721.1/28003.

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36

Stafford, Graham P. "Regulation of methane monooxygenase genes in methanotrophs." Thesis, University of Warwick, 2002. http://wrap.warwick.ac.uk/105607/.

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Methanotrophs are bacteria capable of using methane as their sole carbon and energy source. Oxidation of methane by Methylosinus trichosporium OB3b is catalysed by the particulate (pMMO) and soluble (sMMO) methane monooxygenase enzymes. Transcription of the genes encoding pMMO (pmo) occurs at high copper-to-biomass ratio and sMMO (mmo) at low copper-to-biomass ratios. The aim of this work was to study the regulation of methane monooxygenase gene expression in response to copper ions- the "copper switch". Primer extension and RT-PCR revealed putative transcriptional start sites 5' of the pmoC g
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37

Bradburne, James Andrew. "Regulation of nif gene expression in bradyrhizobium japonicum." Diss., Georgia Institute of Technology, 1992. http://hdl.handle.net/1853/25742.

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38

Husain, Philip Anwar. "Investigative enzymology of selected monooxygenases and development of (S)-N-Succinimidyl-a-Methoxyphenylacetate as a novel tool for assignment of absolute configuration." Diss., Georgia Institute of Technology, 1992. http://hdl.handle.net/1853/27579.

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39

Abdurachim, Kholis Ellis Holly R. "Studies to elucidate the mechanism of reduced flavin transfer in the alkanesulfonate monooxygenase system from Escherichi coli." Auburn, Ala., 2007. http://repo.lib.auburn.edu/2007%20Fall%20Dissertations/Abdurachim_Kholis_37.pdf.

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40

Dorr, Arthur. "The production of cytochrome P-450 by Saccharomyces cerevisiae during computer-controlled batch fermentations." Thesis, University of Surrey, 1991. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.279655.

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41

Veeravalli, S. K. "Flavin-containing monooxygenases : a role in energy homeostasis." Thesis, University College London (University of London), 2011. http://discovery.ucl.ac.uk/1334688/.

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Mice lacking flavin-containing mono-oxygenases (FMOs) genes, Fmos 1, 2 and 4, which are 10-weeks of age, appear healthy, are lean and weigh less than wild-type mice. The knockout mice store less fat in white adipose tissue and have higher HDL cholesterol, glucose and nitric oxide in plasma. Indirect calorimetry results showed that the knockout mice have a higher resting metabolic rate. They also have an increased capacity for voluntary exercise and a higher rate of beta-oxidation in resting soleus muscle. There was no evidence for an increase in adaptive thermogenesis in the knockout mice. Qua
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42

Balke, Kathleen [Verfasser]. "Protein Engineering of Baeyer-Villiger Monooxygenases / Kathleen Balke." Greifswald : Universitätsbibliothek Greifswald, 2018. http://d-nb.info/1150337478/34.

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43

Bufkin, Kendra Bernice. "Mechanistic Studies and Inhibition of N-hydroxylating Monooxygenases." Thesis, Virginia Tech, 2017. http://hdl.handle.net/10919/85845.

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N-hydroxylating monooxygenases (NMO) are members the class B flavoprotein monooxygenases. They catalyze the N-hydroxylation of lysine and ornithine and play and essential role in the biosynthesis of hydroxamate containing siderophores. Siderophores are high affinity iron-chelators composed of catechol and hydroxamate functional groups that are synthesized and secreted by several microorganisms and plants. It has been showed that many NMOs are essential for virulence in many opportunistic pathogens such as Aspergillus fumigatus and Pseudomonas aeruginosa. The focus of my research is on the N-h
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44

Chow, Cathy Sze-Yu. "Selective hydroxylations catalysed by cytochrome P-450 monooxygenases." Thesis, University of Edinburgh, 1998. http://hdl.handle.net/1842/13386.

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The biohydroxylation potential of the mutant enzyme, cytochrome P-450 cam Y96A monooxygenase (Y96A), has been investigated with a series of substrates which differ structurally from that of the natural substrate, D-(+)-camphor. Design of substrates essentially consisted of coupling an aromatic side-chain with an alicyclic moiety <I>via</I> an ester, ether or amide link. Assays have been performed with Y96A in order to obtain data on key factors of the biohydroxylation reaction such as substrate binding and turnover to give hydroxylated products. Y96A research has been complemented by a thoroug
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45

Kunz, Barbara Claudia. "The microsomal monooxygenase system : interactions of the components /." [S.l.] : [s.n.], 1986. http://e-collection.ethbib.ethz.ch/show?type=diss&nr=8084.

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46

Schneider, René Peter. "The NTA-monooxygenase from Pseudomonas sp. ATCC 29600 /." Zürich, 1989. http://e-collection.ethbib.ethz.ch/show?type=diss&nr=8824.

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47

Sowden, Rebecca. "The oxidation of terpenoid hydrocarbons by monooxygenase enzymes." Thesis, University of Oxford, 2003. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.288518.

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48

Basu, Balaka Piku. "The particulate methane monooxygenase from Methylococcus capsulatus (Bath)." Thesis, University of Warwick, 2000. http://wrap.warwick.ac.uk/59505/.

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The isolation procedure for the pMMO complex has been optimised to obtain a high specific activity enzyme from Methylococcus capsulatus (Bath). The enzyme is comprised of the pMMO hydroxylase (pMMOH) consisting of polypeptides 47,26 and 23kDa molecular mass. In addition to this, a putative pMMO reductase (pMMOR) was also found to be necessary to maintain propylene oxidising activity. This component was found to consist of two polypeptides of approximately 63 and 8kDa. Preliminary Nterminal sequence data of the large subunit ofpMMOR indicates that the sequence bears 70% similarity to the methan
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49

Charlton, Susan. "The particulate form of the enzyme methane monooxygenase." Thesis, University of Warwick, 1997. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.323371.

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50

McIntyre, Neil R. "Mechanistic studies of peptidylglycine alpha-amidating monooxygenase (PAM)." [Tampa, Fla] : University of South Florida, 2008. http://purl.fcla.edu/usf/dc/et/SFE0002465.

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