Relevant bibliographies by topics / Flavin hydroquinone dependent Enzymes

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  2. Dissertations / Theses
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Academic literature on the topic 'Flavin hydroquinone dependent Enzymes'

Author: Grafiati
Published: 25 May 2024
Last updated: 31 July 2025

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Journal articles on the topic "Flavin hydroquinone dependent Enzymes"

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Perry, Lynda L., and Gerben J. Zylstra. "Cloning of a Gene Cluster Involved in the Catabolism of p-Nitrophenol by Arthrobacter sp. Strain JS443 and Characterization of the p-Nitrophenol Monooxygenase." Journal of Bacteriology 189, no. 21 (2007): 7563–72. http://dx.doi.org/10.1128/jb.01849-06.

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ABSTRACT The npd gene cluster, which encodes the enzymes of a p-nitrophenol catabolic pathway from Arthrobacter sp. strain JS443, was cloned and sequenced. Three genes, npdB, npdA1, and npdA2, were independently expressed in Escherichia coli in order to confirm the identities of their gene products. NpdA2 is a p-nitrophenol monooxygenase belonging to the two-component flavin-diffusible monooxygenase family of reduced flavin-dependent monooxygenases. NpdA1 is an NADH-dependent flavin reductase, and NpdB is a hydroxyquinol 1,2-dioxygenase. The npd gene cluster also includes a putative maleylacet
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2

Mihasan, Marius, Calin-Bogdan Chiribau, Thorsten Friedrich, Vlad Artenie, and Roderich Brandsch. "An NAD(P)H-Nicotine Blue Oxidoreductase Is Part of the Nicotine Regulon and May Protect Arthrobacter nicotinovorans from Oxidative Stress during Nicotine Catabolism." Applied and Environmental Microbiology 73, no. 8 (2007): 2479–85. http://dx.doi.org/10.1128/aem.02668-06.

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ABSTRACT An NAD(P)H-nicotine blue (quinone) oxidoreductase was discovered as a member of the nicotine catabolic pathway of Arthrobacter nicotinovorans. Transcriptional analysis and electromobility shift assays showed that the enzyme gene was expressed in a nicotine-dependent manner under the control of the transcriptional activator PmfR and thus was part of the nicotine regulon of A. nicotinovorans. The flavin mononucleotide-containing enzyme uses NADH and, with lower efficiency, NADPH to reduce, by a two-electron transfer, nicotine blue to the nicotine blue leuco form (hydroquinone). Besides
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Hyster, Todd K. "Radical Biocatalysis: Using Non-Natural Single Electron Transfer Mechanisms to Access New Enzymatic Functions." Synlett 31, no. 03 (2019): 248–54. http://dx.doi.org/10.1055/s-0037-1611818.

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Exploiting non-natural reaction mechanisms within native enzymes is an emerging strategy for expanding the synthetic capabilities of biocatalysts. When coupled with modern protein engineering techniques, this approach holds great promise for biocatalysis to address long-standing selectivity and reactivity challenges in chemical synthesis. Controlling the stereochemical outcome of reactions involving radical intermediates, for instance, could benefit from biocatalytic solutions because these reactions are often difficult to control by using existing small molecule catalysts. General strategies
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Wojcieszyńska, Danuta, Katarzyna Hupert-Kocurek, and Urszula Guzik. "Flavin-Dependent Enzymes in Cancer Prevention." International Journal of Molecular Sciences 13, no. 12 (2012): 16751–68. http://dx.doi.org/10.3390/ijms131216751.

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Hilvert, Donald, and E. T. Kaisert. "Semisynthetic Enzymes: Design of Flavin-Dependent Oxidoreductases." Biotechnology and Genetic Engineering Reviews 5, no. 1 (1987): 297–318. http://dx.doi.org/10.1080/02648725.1987.10647841.

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Menon, Binuraj R. K., Jonathan Latham, Mark S. Dunstan, et al. "Structure and biocatalytic scope of thermophilic flavin-dependent halogenase and flavin reductase enzymes." Organic & Biomolecular Chemistry 14, no. 39 (2016): 9354–61. http://dx.doi.org/10.1039/c6ob01861k.

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Moon, Shin, and Choe. "Crystal Structures of Putative Flavin Dependent Monooxygenase from Alicyclobacillus Acidocaldarius." Crystals 9, no. 11 (2019): 548. http://dx.doi.org/10.3390/cryst9110548.

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Flavin dependent monooxygenases catalyze various reactions to play a key role in biological processes, such as catabolism, detoxification, and biosynthesis. Group D flavin dependent monooxygenases are enzymes with an Acyl-CoA dehydrogenase (ACAD) fold and use Flavin adenine dinucleotide (FAD) or Flavin mononucleotide (FMN) as a cofactor. In this research, crystal structures of Alicyclobacillus acidocaldarius protein formerly annotated as an ACAD were determined in Apo and FAD bound state. Although our structure showed high structural similarity to other ACADs, close comparison of substrate bin
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Mügge, Carolin, Thomas Heine, Alvaro Gomez Baraibar, Willem J. H. van Berkel, Caroline E. Paul, and Dirk Tischler. "Flavin-dependent N-hydroxylating enzymes: distribution and application." Applied Microbiology and Biotechnology 104, no. 15 (2020): 6481–99. http://dx.doi.org/10.1007/s00253-020-10705-w.

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Shepherd, Sarah A., Chinnan Karthikeyan, Jonathan Latham, et al. "Extending the biocatalytic scope of regiocomplementary flavin-dependent halogenase enzymes." Chemical Science 6, no. 6 (2015): 3454–60. http://dx.doi.org/10.1039/c5sc00913h.

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Saleem-Batcha, Raspudin, Frederick Stull, Jacob N. Sanders, et al. "Enzymatic control of dioxygen binding and functionalization of the flavin cofactor." Proceedings of the National Academy of Sciences 115, no. 19 (2018): 4909–14. http://dx.doi.org/10.1073/pnas.1801189115.

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The reactions of enzymes and cofactors with gaseous molecules such as dioxygen (O2) are challenging to study and remain among the most contentious subjects in biochemistry. To date, it is largely enigmatic how enzymes control and fine-tune their reactions with O2, as exemplified by the ubiquitous flavin-dependent enzymes that commonly facilitate redox chemistry such as the oxygenation of organic substrates. Here we employ O2-pressurized X-ray crystallography and quantum mechanical calculations to reveal how the precise positioning of O2 within a flavoenzyme’s active site enables the regiospeci
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Dissertations / Theses on the topic "Flavin hydroquinone dependent Enzymes"

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Röllig, Robert. "Chemical hydride transfer for flavin dependent monooxygenases of two-component systems." Electronic Thesis or Diss., Aix-Marseille, 2021. http://www.theses.fr/2021AIXM0436.

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Le terme monooxygénases flavoprotéiques (flavoprotein monooxygenases FPMO) recouvre aussi bien des flavoenzymes formées d’une seule composante que de deux. L'indépendance fonctionnelle de la partie oxygénase de la 2,5-dicétocamphane 1,2-monooxygénase I (2,5-DKCMO), une Baeyer-Villiger monooxygénase de type II, FMN dépendante, de sa contrepartie réductase, ainsi que le mécanisme de transfert de la flavine par libre diffusion, ont été étudiés dans des réactions sans réductase mais où des analogues biomimétiques synthétiques de nicotinamide (NCB) ont été utilisés pour réduire le FMN. L'équilibre
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Karunaratne, Kalani Udara. "Probing the methylene and hydride transfers in flavin- dependent thymidylate synthase." Diss., University of Iowa, 2018. https://ir.uiowa.edu/etd/6443.

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All organisms must maintain an adequate level of thymidylate, which gets phosphorylated twice and then utilized by DNA polymerases for DNA replication that must precede cell division. Most organisms rely on classical thymidylate synthase (TSase) for this function. However, a subset of microorganisms – including a number of notable, widespread human pathogens – relies on an enzyme with a distinct structure and catalytic strategy. This enzyme is termed flavin-dependent thymidylate synthase (FDTS), as the flavin is required for thymidylate production. Because of this considerable orthogonality be
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Yuan, Hongling. "Mechanistic Studies of Two Selected Flavin-Dependent Enzymes: Choline Oxidase and D-Arginine Dehydrogenase." Digital Archive @ GSU, 2011. http://digitalarchive.gsu.edu/chemistry_diss/56.

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Choline oxidase catalyzes the flavin-dependent, two-step oxidation of choline to glycine betaine via the formation of an aldehyde intermediate. The oxidation of choline includes two reductive half-reactions followed by oxidative half-reactions. In the first oxidation reaction, the alcohol substrate is activated to its alkoxide via proton abstraction and oxidized via transfer of a hydride from the alkoxide α-carbon to the N(5) atom of the enzyme-bound flavin. In the wild-type enzyme, proton and hydride transfers are mechanistically and kinetically uncoupled. The role of Ser101 was investigated
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Wehelie, Rahma. "Mycoplasma pyrimidine deoxynucleotide biosynthesis : molecular characterization of a new family flavin-dependent thymidylate synthase /." Uppsala : Dept. of Molecular Biosciences, Swedish University of Agricultural Sciences, 2006. http://epsilon.slu.se/200676.pdf.

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Lee, Brendon. "The Role of F420-dependent Enzymes in Mycobacteria." Phd thesis, Canberra, ACT : The Australian National University, 2017. http://hdl.handle.net/1885/148416.

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Tuberculosis (TB) is the leading cause of death by an infectious disease, recently surpassing HIV/AIDS. The causative agent, Mycobacterium tuberculosis, is difficult to treat as it can survive harsh conditions and can switch between an active infection, which causes ~1.5 million deaths a year, and a latent state, which infects up to one third of the world’s population. M. tuberculosis is also becoming more resistant to frontline drugs, making it a dangerous world epidemic. It is therefore essential that new treatments are developed to help combat TB. A
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Goldman, Peter John. "The roles of redox active cofactors in catalysis : structural studies of iron sulfur cluster and flavin dependent enzymes." Thesis, Massachusetts Institute of Technology, 2013. http://hdl.handle.net/1721.1/82313.

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Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Chemistry, 2013.<br>Cataloged from PDF version of thesis.<br>Includes bibliographical references.<br>Cofactors are highly prevalent in biological systems and have evolved to take on many functions in enzyme catalysis. Two cofactors, flavin adenine dinucleotide (FAD) and [4Fe-4S] clusters, were originally determined to aid in electron transfer and redox chemistry. However, additional activities for these cofactors continue to be discovered. The study of FAD in the context of rebeccamycin and staurosporine biosynthesis has yielded
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Kubitza, Christian [Verfasser], Axel [Akademischer Betreuer] Scheidig, and Bernd [Gutachter] Clement. "Structural Characterization of Flavin-dependent Monooxygenases from Zonocerus variegatus and the Human Mitochondrial Amidoxime Reducing Component (mARC) – Enzymes involved in Biotransformation / Christian Kubitza ; Gutachter: Bernd Clement ; Betreuer: Axel Scheidig." Kiel : Universitätsbibliothek Kiel, 2018. http://d-nb.info/1237685664/34.

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Books on the topic "Flavin hydroquinone dependent Enzymes"

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Tamanoi, Fuyuhiko, and Pimchai Chaiyen. Flavin-Dependent Enzymes. Elsevier Science & Technology, 2020.

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Tamanoi, Fuyuhiko, and Pimchai Chaiyen. Flavin-Dependent Enzymes. Elsevier Science & Technology Books, 2020.

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Flavin-Dependent Enzymes: Mechanisms, Structures and Applications. Elsevier, 2020. http://dx.doi.org/10.1016/s1874-6047(20)x0002-3.

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Book chapters on the topic "Flavin hydroquinone dependent Enzymes"

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Fagan, Rebecca L., and Bruce A. Palfey. "Flavin-Dependent Enzymes." In Comprehensive Natural Products II. Elsevier, 2010. http://dx.doi.org/10.1016/b978-008045382-8.00135-0.

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Pimviriyakul, Panu, and Pimchai Chaiyen. "Flavin-dependent dehalogenases." In Flavin-Dependent Enzymes: Mechanisms, Structures and Applications. Elsevier, 2020. http://dx.doi.org/10.1016/bs.enz.2020.05.010.

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Pimviriyakul, Panu, and Pimchai Chaiyen. "Overview of flavin-dependent enzymes." In Flavin-Dependent Enzymes: Mechanisms, Structures and Applications. Elsevier, 2020. http://dx.doi.org/10.1016/bs.enz.2020.06.006.

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Saaret, Annica, Arune Balaikaite, and David Leys. "Biochemistry of prenylated-FMN enzymes." In Flavin-Dependent Enzymes: Mechanisms, Structures and Applications. Elsevier, 2020. http://dx.doi.org/10.1016/bs.enz.2020.05.013.

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Phintha, Aisaraphon, Kridsadakorn Prakinee, and Pimchai Chaiyen. "Structures, mechanisms and applications of flavin-dependent halogenases." In Flavin-Dependent Enzymes: Mechanisms, Structures and Applications. Elsevier, 2020. http://dx.doi.org/10.1016/bs.enz.2020.05.009.

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"Copyright." In Flavin-Dependent Enzymes: Mechanisms, Structures and Applications. Elsevier, 2020. http://dx.doi.org/10.1016/s1874-6047(20)30035-4.

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"Contributors." In Flavin-Dependent Enzymes: Mechanisms, Structures and Applications. Elsevier, 2020. http://dx.doi.org/10.1016/s1874-6047(20)30037-8.

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Chaiyen, Pimchai, and Fuyuhiko Tamanoi. "Preface." In Flavin-Dependent Enzymes: Mechanisms, Structures and Applications. Elsevier, 2020. http://dx.doi.org/10.1016/s1874-6047(20)30038-x.

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Hall, Mélanie. "Flavoenzymes for biocatalysis." In Flavin-Dependent Enzymes: Mechanisms, Structures and Applications. Elsevier, 2020. http://dx.doi.org/10.1016/bs.enz.2020.05.001.

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Martin, Caterina, Claudia Binda, Marco W. Fraaije, and Andrea Mattevi. "The multipurpose family of flavoprotein oxidases." In Flavin-Dependent Enzymes: Mechanisms, Structures and Applications. Elsevier, 2020. http://dx.doi.org/10.1016/bs.enz.2020.05.002.

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