Relevant bibliographies by topics / Monooxygenase oxidation

Academic literature on the topic 'Monooxygenase oxidation'

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Published: 10 December 2022
Last updated: 28 January 2023

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Journal articles on the topic "Monooxygenase oxidation"

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Furuya, Toshiki, Mika Hayashi, and Kuniki Kino. "Reconstitution of Active Mycobacterial Binuclear Iron Monooxygenase Complex in Escherichia coli." Applied and Environmental Microbiology 79, no. 19 (July 26, 2013): 6033–39. http://dx.doi.org/10.1128/aem.01856-13.

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ABSTRACTBacterial binuclear iron monooxygenases play numerous physiological roles in oxidative metabolism. Monooxygenases of this type found in actinomycetes also catalyze various useful reactions and have attracted much attention as oxidation biocatalysts. However, difficulties in expressing these multicomponent monooxygenases in heterologous hosts, particularly inEscherichia coli, have hampered the development of engineered oxidation biocatalysts. Here, we describe a strategy to functionally express the mycobacterial binuclear iron monooxygenase MimABCD inEscherichia coli. Sodium dodecyl sulfate-polyacrylamide gel electrophoretic analysis of themimABCDgene expression inE. colirevealed that the oxygenase components MimA and MimC were insoluble. Furthermore, although the reductase MimB was expressed at a low level in the soluble fraction ofE. colicells, a band corresponding to the coupling protein MimD was not evident. This situation rendered the transformedE. colicells inactive. We found that the following factors are important for functional expression of MimABCD inE. coli: coexpression of the specific chaperonin MimG, which caused MimA and MimC to be soluble inE. colicells, and the optimization of themimDnucleotide sequence, which led to efficient expression of this gene product. These two remedies enabled this multicomponent monooxygenase to be actively expressed inE. coli. The strategy described here should be generally applicable to theE. coliexpression of other actinomycetous binuclear iron monooxygenases and related enzymes and will accelerate the development of engineered oxidation biocatalysts for industrial processes.
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Koo, Christopher W., and Amy C. Rosenzweig. "Biochemistry of aerobic biological methane oxidation." Chemical Society Reviews 50, no. 5 (2021): 3424–36. http://dx.doi.org/10.1039/d0cs01291b.

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Methane monooxygenase enzymes use metal cofactors to activate methane under ambient, aerobic conditions. This review highlights recent progress in understanding the structure and activity of the membrane-bound and soluble methane monooxygenases.
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Kostichka, Kristy, Stuart M. Thomas, Katharine J. Gibson, Vasantha Nagarajan, and Qiong Cheng. "Cloning and Characterization of a Gene Cluster for Cyclododecanone Oxidation in Rhodococcus ruber SC1." Journal of Bacteriology 183, no. 21 (November 1, 2001): 6478–86. http://dx.doi.org/10.1128/jb.183.21.6478-6486.2001.

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ABSTRACT Biological oxidation of cyclic ketones normally results in formation of the corresponding dicarboxylic acids, which are further metabolized in the cell. Rhodococcus ruber strain SC1 was isolated from an industrial wastewater bioreactor that was able to utilize cyclododecanone as the sole carbon source. A reverse genetic approach was used to isolate a 10-kb gene cluster containing all genes required for oxidative conversion of cyclododecanone to 1,12-dodecanedioic acid (DDDA). The genes required for cyclododecanone oxidation were only marginally similar to the analogous genes for cyclohexanone oxidation. The biochemical function of the enzymes encoded on the 10-kb gene cluster, the flavin monooxygenase, the lactone hydrolase, the alcohol dehydrogenase, and the aldehyde dehydrogenase, was determined in Escherichia coli based on the ability to convert cyclododecanone. Recombinant E. colistrains grown in the presence of cyclododecanone accumulated lauryl lactone, 12-hydroxylauric acid, and/or DDDA depending on the genes cloned. The cyclododecanone monooxygenase is a type 1 Baeyer-Villiger flavin monooxygenase (FAD as cofactor) and exhibited substrate specificity towards long-chain cyclic ketones (C11 to C15), which is different from the specificity of cyclohexanone monooxygenase favoring short-chain cyclic compounds (C5 to C7).
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van Hylckama Vlieg, Johan E. T., Hans Leemhuis, Jeffrey H. Lutje Spelberg, and Dick B. Janssen. "Characterization of the Gene Cluster Involved in Isoprene Metabolism in Rhodococcus sp. Strain AD45." Journal of Bacteriology 182, no. 7 (April 1, 2000): 1956–63. http://dx.doi.org/10.1128/jb.182.7.1956-1963.2000.

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ABSTRACT The genes involved in isoprene (2-methyl-1,3-butadiene) utilization in Rhodococcus sp. strain AD45 were cloned and characterized. Sequence analysis of an 8.5-kb DNA fragment showed the presence of 10 genes of which 2 encoded enzymes which were previously found to be involved in isoprene degradation: a glutathioneS-transferase with activity towards 1,2-epoxy-2-methyl-3-butene (isoI) and a 1-hydroxy-2-glutathionyl-2-methyl-3-butene dehydrogenase (isoH). Furthermore, a gene encoding a second glutathioneS-transferase was identified (isoJ). TheisoJ gene was overexpressed in Escherichia coliand was found to have activity with 1-chloro-2,4-dinitrobenzene and 3,4-dichloro-1-nitrobenzene but not with 1,2-epoxy-2-methyl-3-butene. Downstream of isoJ, six genes (isoABCDEF) were found; these genes encoded a putative alkene monooxygenase that showed high similarity to components of the alkene monooxygenase fromXanthobacter sp. strain Py2 and other multicomponent monooxygenases. The deduced amino acid sequence encoded by an additional gene (isoG) showed significant similarity with that of α-methylacyl-coenzyme A racemase. The results are in agreement with a catabolic route for isoprene involving epoxidation by a monooxygenase, conjugation to glutathione, and oxidation of the hydroxyl group to a carboxylate. Metabolism may proceed by fatty acid oxidation after removal of glutathione by a still-unknown mechanism.
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Yamamoto, Taisei, Kento Kobayashi, Yoshie Hasegawa, and Hiroaki Iwaki. "Cloning, expression, and characterization of Baeyer–Villiger monooxygenases from eukaryotic Exophiala jeanselmei strain KUFI-6N." Bioscience, Biotechnology, and Biochemistry 85, no. 7 (April 30, 2021): 1675–85. http://dx.doi.org/10.1093/bbb/zbab079.

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ABSTRACT The fungus Exophiala jeanselmei strain KUFI-6N produces a unique cycloalkanone monooxygenase (ExCAMO) that displays an uncommon substrate spectrum of Baeyer–Villiger oxidation of 4-10-membered ring ketones. In this study, we aimed to identify and sequence the gene encoding ExCAMO from KUFI-6N and overexpress the gene in Escherichia coli. We found that the primary structure of ExCAMO is most closely related to the cycloalkanone monooxygenase from Cylindrocarpon radicicola ATCC 11011, with 54.2% amino acid identity. ExCAMO was functionally expressed in E. coli and its substrate spectrum and kinetic parameters were investigated. Substrate profiling indicated that ExCAMO is unusual among known Baeyer–Villiger monooxygenases owing to its ability to accept a variety of substrates, including C4-C12 membered ring ketones. ExCAMO has high affinity and catalytic efficiency toward cycloalkanones, the highest being toward cyclohexanone. Five other genes encoding Baeyer–Villiger monooxygenases were also cloned and expressed in E. coli.
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Brzostowicz, Patricia C., Dana M. Walters, Stuart M. Thomas, Vasantha Nagarajan, and Pierre E. Rouvière. "mRNA Differential Display in a Microbial Enrichment Culture: Simultaneous Identification of Three Cyclohexanone Monooxygenases from Three Species." Applied and Environmental Microbiology 69, no. 1 (January 2003): 334–42. http://dx.doi.org/10.1128/aem.69.1.334-342.2003.

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ABSTRACT mRNA differential display has been used to identify cyclohexanone oxidation genes in a mixed microbial community derived from a wastewater bioreactor. Thirteen DNA fragments randomly amplified from the total RNA of an enrichment subculture exposed to cyclohexanone corresponded to genes predicted to be involved in the degradation of cyclohexanone. Nine of these DNA fragments are part of genes encoding three distinct Baeyer-Villiger cyclohexanone monooxygenases from three different bacterial species present in the enrichment culture. In Arthrobacter sp. strain BP2 and Rhodococcus sp. strain Phi2, the monooxygenase is part of a gene cluster that includes all the genes required for the degradation of cyclohexanone, while in Rhodococcus sp. strain Phi1 the genes surrounding the monooxygenase are not predicted to be involved in this degradation pathway but rather seem to belong to a biosynthetic pathway. Furthermore, in the case of Arthrobacter strain BP2, three other genes flanking the monooxygenase were identified by differential display, demonstrating that the repeated sampling of bacterial operons shown earlier for a pure culture (D. M. Walters, R. Russ, H. Knackmuss, and P. E. Rouvière, Gene 273:305-315, 2001) is also possible for microbial communities. The activity of the three cyclohexanone monooxygenases was confirmed and characterized following their expression in Escherichia coli.
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Willetts, Andrew. "The Isoenzymic Diketocamphane Monooxygenases of Pseudomonas putida ATCC 17453—An Episodic History and Still Mysterious after 60 Years." Microorganisms 9, no. 12 (December 15, 2021): 2593. http://dx.doi.org/10.3390/microorganisms9122593.

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Researching the involvement of molecular oxygen in the degradation of the naturally occurring bicyclic terpene camphor has generated a six-decade history of fascinating monooxygenase biochemistry. While an extensive bibliography exists reporting the many varied studies on camphor 5-monooxygenase, the initiating enzyme of the relevant catabolic pathway in Pseudomonas putida ATCC 17453, the equivalent recorded history of the isoenzymic diketocamphane monooxygenases, the enzymes that facilitate the initial ring cleavage of the bicyclic terpene, is both less extensive and more enigmatic. First referred to as ‘ketolactonase—an enzyme for cyclic lactonization’—the enzyme now classified as 2,5-diketocamphane 1,2-monooxygenase (EC 1.14.14.108) holds a special place in the history of oxygen-dependent biochemistry, being the first biocatalyst confirmed to undertake a biooxygenation reaction equivalent to the peracid-catalysed Baeyer–Villiger chemical oxidation first reported in the late 19th century. However, following that auspicious beginning, the biochemistry of EC 1.14.14.108, and its isoenzymic partner 3,6-diketocamphane 1,6-monooxygenase (EC 1.14.14.155) was dogged for many years by the mistaken belief that the enzymes were true flavoproteins that function with a tightly-bound flavin cofactor in the active site. This misconception led to a number of erroneous interpretations of relevant experimental data. It is only in the last decade, initially as the result of pure serendipity, that these enzymes have been confirmed to be members of a relatively recently discovered class of oxygen-dependent enzymes, the flavin-dependent two-component monooxygenases. This has promoted a renaissance of interest in the enzymes, resulting in programmes of research that have significantly expanded current knowledge of both their mode of action and regulation in camphor-grown P. putida ATCC 17453. However, some features of the biochemistry of the isoenzymic diketocamphane monooxygenases remain currently unexplained. It is the episodic history of these enzymes and some of what remains unresolved that are the principal subjects of this review.
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Brzostowicz, Patricia C., Katharine L. Gibson, Stuart M. Thomas, Mary Sue Blasko, and Pierre E. Rouvière. "Simultaneous Identification of Two Cyclohexanone Oxidation Genes from an Environmental Brevibacterium Isolate Using mRNA Differential Display." Journal of Bacteriology 182, no. 15 (August 1, 2000): 4241–48. http://dx.doi.org/10.1128/jb.182.15.4241-4248.2000.

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ABSTRACT The technique of mRNA differential display was used to identify simultaneously two metabolic genes involved in the degradation of cyclohexanone in a new halotolerant Brevibacteriumenvironmental isolate. In a strategy based only on the knowledge that cyclohexanone oxidation was inducible in this strain, the mRNA population of cells exposed to cyclohexanone was compared to that of control cells using reverse transcription-PCR reactions primed with a collection of 81 arbitrary oligonucleotides. Three DNA fragments encoding segments of flavin monooxygenases were isolated with this technique, leading to the identification of the genes of two distinct cyclohexanone monooxygenases, the enzymes responsible for the oxidation of cyclohexanone. Each monooxygenase was expressed in Escherichia coli and characterized. This work validates the application of mRNA differential display for the discovery of new microbial metabolic genes.
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Brantner, Christine A., Lorie A. Buchholz, Claudia L. McSwain, Laura L. Newcomb, Charles C. Remsen, and Mary Lynne Perille Collins. "Intracytoplasmic membrane formation in Methylomicrobium album BG8 is stimulated by copper in the growth medium." Canadian Journal of Microbiology 43, no. 7 (July 1, 1997): 672–76. http://dx.doi.org/10.1139/m97-095.

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Methylomicrobium album BG8 uses methane as its sole source of carbon and energy. The oxidation of methane to methanol is catalyzed by the enzyme methane monooxygenase. Methane monooxygenase activity, intracytoplasmic membrane abundance, and cell mass increased with increasing copper concentration in the medium. When copper was added to copper-deficient cultures, cell mass and intracytoplasmic membrane structure increased. These findings are consistent with the presence of copper in the particulate methane monooxygenase. Methane monooxygenase activity and intracytoplasmic membrane abundance were correlated, suggesting that the methane monooxygenase may be involved in intracytoplasmic membrane proliferation.Key words: Methylomicrobium album BG8, copper, intracytoplasmic membrane, methane monooxygenase.
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Hamamura, Natsuko, Ryan T. Storfa, Lewis Semprini, and Daniel J. Arp. "Diversity in Butane Monooxygenases among Butane-Grown Bacteria." Applied and Environmental Microbiology 65, no. 10 (October 1, 1999): 4586–93. http://dx.doi.org/10.1128/aem.65.10.4586-4593.1999.

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ABSTRACT Butane monooxygenases of butane-grown Pseudomonas butanovora, Mycobacterium vaccae JOB5, and an environmental isolate, CF8, were compared at the physiological level. The presence of butane monooxygenases in these bacteria was indicated by the following results. (i) O2 was required for butane degradation. (ii) 1-Butanol was produced during butane degradation. (iii) Acetylene inhibited both butane oxidation and 1-butanol production. The responses to the known monooxygenase inactivator, ethylene, and inhibitor, allyl thiourea (ATU), discriminated butane degradation among the three bacteria. Ethylene irreversibly inactivated butane oxidation by P. butanovora but not by M. vaccae or CF8. In contrast, butane oxidation by only CF8 was strongly inhibited by ATU. In all three strains of butane-grown bacteria, specific polypeptides were labeled in the presence of [14C]acetylene. The [14C]acetylene labeling patterns were different among the three bacteria. Exposure of lactate-grown CF8 and P. butanovora and glucose-grownM. vaccae to butane induced butane oxidation activity as well as the specific acetylene-binding polypeptides. Ammonia was oxidized by all three bacteria. P. butanovora oxidized ammonia to hydroxylamine, while CF8 and M. vaccae produced nitrite. All three bacteria oxidized ethylene to ethylene oxide. Methane oxidation was not detected by any of the bacteria. The results indicate the presence of three distinct butane monooxygenases in butane-grown P. butanovora, M. vaccae, and CF8.
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Dissertations / Theses on the topic "Monooxygenase oxidation"

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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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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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Maurer, Steffen Christian. "Oxidationsreaktionen mittels der Cytochrom P450-Monooxygenase CYP102A1 in Enzymreaktoren." [S.l. : s.n.], 2006. http://nbn-resolving.de/urn:nbn:de:bsz:93-opus-28118.

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Hogan, Matthew Charles. "Process issues in redox biocatalysis : cyclohexanone monooxygenase catalysed chiral lactone syntheses." Thesis, University College London (University of London), 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.325655.

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Pilkington, Simon John. "The soluble methane monooxygenase and ammonia oxidation in the obligate methanotroph 'Methylosinus trichosporium (OB3b)'." Thesis, University of Warwick, 1986. http://wrap.warwick.ac.uk/66751/.

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The aim of this project was to isolate and characterise the soluble methane monooxygenase (MMO) from the obligate methanotroph Methylosinus trichosporium (OB3b) and to investigate its role in the oxidation of ammonia. The nature and location of the MMO was shown to be dependent on the availability of copper to the organism. Cells grown in chemostat culture with copper in excess produced a particulate MMO. whereas under conditions of copper stress a soluble MMO is ,produced. This response was independent of the carbon and energy source used for growth (methane or methanol). The soluble MMO was separated into two fractions by DEAE ion exchange chromatography. Each had no MMO activity when assayed individually but had MMO activity when assayed in combination. Fraction A consisted of material that failed to bind to DEAE cellulose and from it component A of the soluble MMOwas purified. Component A had an Mr of 230000 and consisted of three subunits a, B and Y of Mr 54000. 40000 and 18500 respectively. suggesting a a2B2Y2 subunit structure. Component A could replace component A of the soluble MMO of Methylococcus capsulatus (Bath) in assays of pure components of the soluble MMO from this organism and was therefore identified as the hydroxylase component of the enzyme. Fraction C consisted Of material eluted from DEAE cellulose by 0.3 M NaC1, from it component C of the soluble MMO was partially purified. Component C was purified to a point where it consisted predominantly of two proteins of Mr 38000 and 58000. Component C could replace component C of the soluble MMO of Methylococcus capsulatus (Bath) in MMO assays of pure components of the soluble MMO from this organism and was therefore identified as the NADH:acceptor reductase component of the enzyme. The presence of a third component (component B) of the soluble MMO essential for MMO activity was demonstrated. Component B was not purified or isolated from components A or C but it was 'shown to be analogous to component B of the soluble MMO of MethYlococcus capsulatus (Bath). The close functional and physicochemical similarity between the components of the soluble MMOs from Methylosinus trichosporium (OB3b) and Methylococcus capsulatus (Bath) is discussed. as is the distinct difference between the soluble and particulate MMOs from Methylosinus trichosporium (OB3b). The soluble MMOwas shown to oxidise ammonia to hydroxylamine in that: 1. ammonia oxidation required the presence of NAD(P)H for activity as does the soluble MMO; 2. ammonia oxidation was inhibited by acetylene and 8-hydroxyquinoline. specific inhibitors of the soluble MMO. 3. Ammonia oxidation required the presence of both DEAE fractions of the soluble MMO for activity. and U. ammonia oxidation activity was always associated with the soluble MMO and was never present in extracts lacking soluble MMO activity. Hydroxylamine inhibits the soluble MMO (50% at 1,mM) and this was identified as a cause of the cessation of maximum ammonia oxidising activity after 1 minute 1n vitro. Only low levels of hydroxylamine oxidoreductase activity were measured in vitro (> 1 nmol/min/mg) and activity failed to be stimulated by the addition of a number of electron donors.
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Keppler, Artur Franz. "Biotransformações de cetonas aromáticas e cíclicas promovidas por fungos." Universidade de São Paulo, 2005. http://www.teses.usp.br/teses/disponiveis/46/46135/tde-13032007-123741/.

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Nesse trabalho avaliamos o potencial enzimático de diferentes linhagens de fungos, visando determinar a presença de mono-oxigenases capazes de oxidar cetonas aromáticas e cíclicas. Todas as linhagens empregadas apresentaram atividade de álcool desidrogenase e Baeyer-Villiger mono-oxigenases. Adicionalmente foram sintetizadas oito moléculas bi-funcionalizadas com grupos sulfeto, seleneto e carbonila (cetona). Os produtos das reações biocatalisadas foram isolados e caracterizados.
In this work, we evaluated the enzymatic potential of different Aspergillus strains, through the biotransformations of two substrates: 2- and 4-methylcyclohexanone (1a e 1b). All the strains employed showed alcohol dehydrogenase and Baeyer-Villiger monooxygenase (CPMO and CHMO) activities. These enzymes can perform ketone biorreduction and oxidation. Using the A. terreus SSP 1498 selected from the screening study, we prepared alcohols and lactones in good enantiosselectivity. In this way, other fungal strains were studied aiming to determine the presence of monooxygenase activity by means of the biotransformation of aromatic ketones. Like the Aspergillus, we observed that all strains used in this study showed alcohol dehydrogenase and Baeyer-Villiger monooxygenase (APMO) activities. We selected 1-phenyl-etanone and its para substituted derivates as substrates. Additionally, we synthesized eight examples of bi-functionalized compounds with sulfide, selenide and ketone groups. These compounds were submitted to the action of enzymatic system of different fungi which were selected from the initial screening. The products from the biotransformation were isolated and characterized.
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Valentine, Ann M. (Ann Margaret) 1971. "Bioinorganic hydrocarbon oxidation : mechanistic and kinetic studies of the soluble methane monooxygenase from Methylococcus capsulates (bath)." Thesis, Massachusetts Institute of Technology, 1998. http://hdl.handle.net/1721.1/50508.

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Thesis (Ph.D.)--Massachusetts Institute of Technology, Dept. of Chemistry, 1998.
Includes bibliographical references (p. 219-233).
Chapter 1. Principles of Small Molecule Activation by Metalloproteins as Exemplified by the Soluble Methane Monooxygenase -- Chapter 2. Small Molecule Binding to the Mixed-Valent Diiron Center of Methane Monooxygenase Hydroxylase from Methylococcus capsulatus (Bath) as Revealed by ENDOR Spectroscopy -- Chapter 3. An EPR Study of the Dinuclear Iron Site in the Soluble Methane Monooxygenase Reduced by One Electron at 77 K: the Effect of Component Interactions and the Binding of Small Molecules to the Dinuclear Ferric Center -- Chapter 4. An Investigation of the Reaction of Diferrous Methane Monooxygenase Hydroxylase with Dioxygen and Substrates by Rapid Freeze- Quench and Stopped-Flow Spectroscopy -- Chapter 5. Oxidation of Radical Clock Substrate Probes by the Soluble Methane Monooxygenase System -- Chapter 6. Tritiated Chiral Alkanes as Probes for the Mechanism of Hydroxylation by the Soluble Methane Monooxygenase.
by Ann M. Valentine.
Ph.D.
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Harrison, John Samuel. "Production and characterisation of dioxygenase- and monooxygenase-catalysed oxidation products from a range of arenes and oxaarenes." Thesis, Queen's University Belfast, 1999. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.301717.

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Mohanty, Sujit Kumar. "A. Genetic characterization of the caffeine C-8 oxidation pathway in Pseudomonas Sp. CBB1 B. Validation of caffeine dehydrogenase as a suitable enzyme for a rapid caffeine diagnostic test." Diss., University of Iowa, 2013. https://ir.uiowa.edu/etd/4879.

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Pseudomonassp. CBB1 degraded caffeine via C-8 oxidation. Previously, a novel quinone-dependent caffeine dehydrogenase (Cdh) was shown to catalyze the oxidation of caffeine to 1,3,7-trimethyluric acid (TMU). Initial metabolite analysis using resting cells and partially purified extract of CBB1 identified transient accumulation 1,3,7-trimethyl-5-hydroxyisourate (TM-HIU), and 3,6,8-trimethylallantoin (TMA). TMA structure was confirmed; chiral analysis revealed that it was racemic. In contrast, a time-course reaction showed that one of the enantiomers of TMA accumulated nine times, and racemized in three hours. Based on this, it was proposed that TMU was converted to TM-HIU and enantiomeric TMA. A 43-kDa NADH-dependent TMU mononxygenase (TmuM) was purified and shown to convert TMU to unstable TM-HIU. The enzyme belonged to a new family of FAD-dependent monooxygenases. The enzyme was specific for methyluric acid with no activity on uric acid. Homology model of TmuM revealed a larger, more hydrophobic active site compared to analogous uricase in the uric acid pathway. Genes encoding heterotrimeric Cdh (cdhA,B,C) and TmuM (tmuM), were located on a 25.2-kb fragment in CBB1 genome. Gene cluster analysis relative to similar cluster in uric acid degrading organisms identified five more putative genes of the C-8 oxidation pathway, namely tmuH, tmuD, orf1, orf2, and orf3. First three genes were assigned encoding TM-HIU hydrolase (TM-HIU to TM-OHCU), TM-OHCU decarboxylase (TM-OHCU to stereospecific TMA (proposed S-(+)-TMA)), and trimethylallantoinase (stereospecific TMA to TMAA), respectively. Further, orf2 and orf3 are proposed to encode for YlbA and ArgE like hydrolase and deacetylase, which convert TMAA to glyoxylate, di- and monomethylurea. This is the first report of (a) TMA structure (b) TMU monooxygenase and TM-HIU (hydroxylation product of TMU), and (c) complete delineation of C-8 oxidation pathway by a combination of enzymology and cluster analysis. Excessive consumption of caffeine in various forms has created a need for a rapid diagnostic test, esp. for nursing mothers and infants. Cdh was hypothesized to be suitable for this test. Sensitivity of the test was shown to be 1 ppm. A colorimetric test with partially purified Cdh and INT-dye was optimized to detect within a minute, caffeine in drugs, nursing mother's milk, and differentiate decaffeinated beverages.
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Ray, Anirban. "Identification, Enumeration and Diversity of Nitrifying Bacteria in the Laurentian Great Lakes." Bowling Green State University / OhioLINK, 2012. http://rave.ohiolink.edu/etdc/view?acc_num=bgsu1351276518.

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Books on the topic "Monooxygenase oxidation"

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Pilkington, S. J. The soluble methane monooxygenase and ammonia oxidation in the obligate methanotroph "Methylosinus trichosporium (OB3b)". [s.l.]: typescript, 1986.

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1942-, Schmid Rolf, and Urlacher Vlada B, eds. Modern biooxidation: Enzymes, reactions, and applications. Weinheim: Wiley-VCH, 2007.

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NATO Advanced Study Institute on Molecular Aspects of Drug Metabolizing Enzymes (1993 Kuşadası, Turkey). Molecular aspects of oxidative drug metabolizing enzymes: Their significance in environmental toxicology, chemical carcinogenesis, and health. Berlin: Springer-Verlag,in cooperation with NATO Scientific Affairs Division, 1995.

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Emel, Arinç, Schenkman John B, and Hodgson Ernest 1932-, eds. Molecular and applied aspects of oxidative drug metabolizing enzymes. New York: Plenum Press, 1999.

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Modern biooxidation: Enzymes, reactions and applications. Weinheim, DE: Wiley-VCH, 2008.

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Emel, Arinç, Schenkman John B, Hodgson Ernest 1932-, and NATO Advanced Study Institute on Molecular Aspects of Drug Metabolizing Enzymes (1993 : Kus̜adası, Turkey), eds. Molecular aspects of oxidative drug metabolizing enzymes: Their significance in environmental toxicology, chemical carcinogenesis, and health. Berlin: Springer-Verlag, 1995.

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Arinc, Emel, John B. Schenkman, and Ernest Hodgson. Molecular Aspects of Oxidative Drug Metabolizing Enzymes: Their Significance in Environmental Toxicology, Chemical Carcinogenesis and Health. Springer London, Limited, 2013.

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Schenkman, John B. Molecular Aspects of Oxidative Drug Metabolizing Enzymes: Their Significance in Environmental Toxicology, Chemical Carcinogenesis and Health (Nato a S I Series Series H, Cell Biology). Springer-Verlag Telos, 1995.

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Book chapters on the topic "Monooxygenase oxidation"

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Liu, Katherine E., Andrew L. Feig, David P. Goldberg, Stephen P. Watton, and Stephen J. Lippard. "Methane Monooxygenase: Models and Mechanism." In The Activation of Dioxygen and Homogeneous Catalytic Oxidation, 301–20. Boston, MA: Springer US, 1993. http://dx.doi.org/10.1007/978-1-4615-3000-8_22.

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Rosenzweig, Amy C., Xudong Feng, and Stephen J. Lippard. "Studies of Methane Monooxygenase and Alkane Oxidation Model Complexes." In Applications of Enzyme Biotechnology, 69–85. Boston, MA: Springer US, 1991. http://dx.doi.org/10.1007/978-1-4757-9235-5_6.

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Grechkin, A. N., T. E. Gafarova, O. S. Korolev, R. A. Kuramshin, and I. A. Tarchevsky. "The Monooxygenase Pathway of Linoleic Acid Oxidation in Pea Seedlings." In Biological Role of Plant Lipids, 83–85. Boston, MA: Springer US, 1989. http://dx.doi.org/10.1007/978-1-4684-1303-8_18.

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Girhard, Marco, and Vlada B. Urlacher. "Biooxidation with Cytochrome P450 Monooxygenases." In Modern Oxidation Methods, 421–50. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2010. http://dx.doi.org/10.1002/9783527632039.ch12.

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Colonna, S., N. Gaggero, C. Richelmi, and P. Pasta. "Enantioselective Oxidations Catalyzed by Peroxidases and Monooxygenases." In Enzymes in Action, 133–60. Dordrecht: Springer Netherlands, 2000. http://dx.doi.org/10.1007/978-94-010-0924-9_7.

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Addison, Richard F. "Monooxygenase Measurements as Indicators of Pollution in the Field." In Molecular Aspects of Oxidative Drug Metabolizing Enzymes, 549–65. Berlin, Heidelberg: Springer Berlin Heidelberg, 1995. http://dx.doi.org/10.1007/978-3-642-79528-2_27.

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Schenkman, John B., Ingela Jansson, Gary Davis, Paul P. Tamburini, Zhongqing Lu, Zhe Zhang, and James F. Rusling. "Protein-Protein Interactions in the P450 Monooxygenase System." In Molecular and Applied Aspects of Oxidative Drug Metabolizing Enzymes, 21–39. Boston, MA: Springer US, 1999. http://dx.doi.org/10.1007/978-1-4615-4855-3_2.

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Hodgson, Ernest, Nathan J. Cherrington, Richard M. Philpot, and Randy L. Rose. "Biochemical Aspects of Flavin-Containing Monooxygenases (FMOs)." In Molecular and Applied Aspects of Oxidative Drug Metabolizing Enzymes, 55–70. Boston, MA: Springer US, 1999. http://dx.doi.org/10.1007/978-1-4615-4855-3_4.

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Philpot, Richard M., Christine P. Biagini, Geraldine T. Carver, Lila H. Overby, M. Keith Wyatt, and Kiyoshi Itagaki. "Expression and Regulation of Flavin-Containing Monooxygenases." In Molecular and Applied Aspects of Oxidative Drug Metabolizing Enzymes, 71–79. Boston, MA: Springer US, 1999. http://dx.doi.org/10.1007/978-1-4615-4855-3_5.

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Hodgson, Ernest, Bonnie L. Blake, Patricia E. Levi, Richard B. Mailman, Michael P. Lawton, Richard M. Philpot, and Mary Beth Genter. "Flavin-Containing Monooxygenases: Substrate Specificity and Complex Metabolic Pathways." In Molecular Aspects of Oxidative Drug Metabolizing Enzymes, 225–35. Berlin, Heidelberg: Springer Berlin Heidelberg, 1995. http://dx.doi.org/10.1007/978-3-642-79528-2_12.

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Conference papers on the topic "Monooxygenase oxidation"

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Brondani, Patrícia B., Gonzalo de Gonzalo, Marco W. Fraaije, and Leandro H. Andrade. "Selective oxidations of organoboron compounds catalyzed by Baeyer-Villiger monooxygenases." In 14th Brazilian Meeting on Organic Synthesis. São Paulo: Editora Edgard Blücher, 2013. http://dx.doi.org/10.5151/chempro-14bmos-r0097-2.

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You might also be interested in the extended bibliographies on the topic 'Monooxygenase oxidation' for particular source types:
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