Relevant bibliographies by topics / Copper. Amine oxidase. Quinone

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters

Academic literature on the topic 'Copper. Amine oxidase. Quinone'

Author: Grafiati
Published: 4 June 2021
Last updated: 18 February 2022

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'Copper. Amine oxidase. Quinone.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Journal articles on the topic "Copper. Amine oxidase. Quinone"

1

Wilmot, C. M. "Oxygen activation in a copper-containing amine oxidase." Biochemical Society Transactions 31, no. 3 (2003): 493–96. http://dx.doi.org/10.1042/bst0310493.

Full text
Abstract:
The process by which molecular oxygen is activated to enable it to function as an electron acceptor in biology is poorly understood. The quinoprotein copper-containing amine oxidase (CuAO) catalyses the conversion of primary amines into aldehydes. As well as copper, the enzyme contains an organic cofactor, 2,4,5-trihydroxyphenylalanine quinone (TPQ). Following the formation of aldehyde, the enzyme is left as the two-electron reduced aminoquinol form. Reoxidation of the enzyme back to the resting state uses molecular oxygen, which is reduced to H2O2 in the process, with the additional release o
APA, Harvard, Vancouver, ISO, and other styles
2

Collison, D., P. F. Knowles, F. E. Mabbs, et al. "Studies on the active site of pig plasma amine oxidase." Biochemical Journal 264, no. 3 (1989): 663–69. http://dx.doi.org/10.1042/bj2640663.

Full text
Abstract:
Amine oxidase from pig plasma (PPAO) has two bound Cu2+ ions and at least one pyrroloquinoline quinone (PQQ) moiety as cofactors. It is shown that recovery of activity by copper-depleted PPAO is linear with respect to added Cu2+ ions. Recovery of e.s.r. and optical spectral characteristics of active-site copper parallel the recovery of catalytic activity. These results are consistent with both Cu2+ ions contributing to catalysis. Further e.s.r. studies indicate that the two copper sites in PPAO, unlike those in amine oxidases from other sources, are chemically distinct. These comparative studi
APA, Harvard, Vancouver, ISO, and other styles
3

Cooper, R. A., P. F. Knowles, D. E. Brown, M. A. McGuirl, and D. M. Dooley. "Evidence for copper and 3,4,6-trihydroxyphenylalanine quinone cofactors in an amine oxidase from the gram-negative bacterium Escherichia coli K-12." Biochemical Journal 288, no. 2 (1992): 337–40. http://dx.doi.org/10.1042/bj2880337.

Full text
Abstract:
The cofactors present in a amine oxidase induced in Escherichia coli K-12 by growth on 2-phenylethylamine have been studied by spectroscopic methods. E.s.r. spectroscopy establishes the presence of cupric copper while resonance Raman spectroscopy on the phenylhydrazine derivative of the enzyme provides strong evidence for the oxidized form of 3,4,6-trihydroxyphenylalanine (TOPA) quinone. The amine oxidase should accordingly be classified as EC 1.4.3.6. This is the first report of such an amine oxidase in a Gram-negative bacterium.
APA, Harvard, Vancouver, ISO, and other styles
4

Largeron, Martine. "Aerobic catalytic systems inspired by copper amine oxidases." Pure and Applied Chemistry 92, no. 2 (2020): 233–42. http://dx.doi.org/10.1515/pac-2019-0107.

Full text
Abstract:
AbstractThe goal of sustainable development has been accepted as a common policy in current society. In response to this challenge, the development of green processes which utilize environmentally benign oxidants, reduce chemical waste and handling costs, is highly desirable. Given the widespread importance of imines as pivotal synthetic intermediates and essential pharmacophores in numerous biologically active compounds, various catalytic methods allowing the aerobic oxidation of amines to imines have been developed. Recently, noticeable progress has arisen from the discovery of various quino
APA, Harvard, Vancouver, ISO, and other styles
5

McGuirl, M. A., D. E. Brown, C. D. McCahon, P. N. Turowski, and D. M. Dooley. "Copper-quinone interactions in amine oxidases." Journal of Inorganic Biochemistry 43, no. 2-3 (1991): 186. http://dx.doi.org/10.1016/0162-0134(91)84178-c.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

TANIZAWA, Katsuyuki. "Molecular Mechanism of Topa Quinone Biogenesis in Copper Amine Oxidase." Kagaku To Seibutsu 35, no. 8 (1997): 569–75. http://dx.doi.org/10.1271/kagakutoseibutsu1962.35.569.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

Kim, M., T. Okajima, S. Kishishita, et al. "X-ray snapshots of quinone cofactor biogenesis in bacterial copper amine oxidase." Acta Crystallographica Section A Foundations of Crystallography 58, s1 (2002): c298. http://dx.doi.org/10.1107/s0108767302096915.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Mura, Anna, Alessandra Padiglia, Rosaria Medda, Francesca Pintus, Alessandro Finazzi Agrò, and Giovanni Floris. "Properties of copper-free pig kidney amine oxidase: Role of topa quinone." FEBS Letters 580, no. 18 (2006): 4317–24. http://dx.doi.org/10.1016/j.febslet.2006.06.089.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

Klinman, Judith P. "The multi-functional topa-quinone copper amine oxidases." Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1647, no. 1-2 (2003): 131–37. http://dx.doi.org/10.1016/s1570-9639(03)00077-3.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

Largeron, Martine. "Aerobic catalytic systems inspired by copper amine oxidases: recent developments and synthetic applications." Organic & Biomolecular Chemistry 15, no. 22 (2017): 4722–30. http://dx.doi.org/10.1039/c7ob00507e.

Full text
Abstract:
Recently, chemists have developed aerobic quinone-based catalytic systems in order to reproduce enzymatic activity and selectivity of copper amine oxidases but also to expand the scope of amine substrates.
APA, Harvard, Vancouver, ISO, and other styles
More sources

Dissertations / Theses on the topic "Copper. Amine oxidase. Quinone"

1

Shepard, Eric Michael. "Understanding the molecular factors governing inhibitor potency and oxygen activation in copper amine oxidases." Diss., Montana State University, 2006. http://etd.lib.montana.edu/etd/2006/shepard/ShepardE0506.pdf.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Juda, Gregory Alexander. "Mechanism and inhibition of the phenylethylamine oxidase from Arthrobacter globiformis." Diss., Montana State University, 2005. http://etd.lib.montana.edu/etd/2005/juda/JudaG0505.pdf.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Johnson, Steven A. "Spectroscopic studies of copper amine oxidase." Thesis, University of Salford, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.300884.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Green, Edward L. "Characterization of the TPQ cofactor in amine oxidases and the heme cofactor in cystathionine beta-synthase by resonance raman spectroscopy. : Implications for catalytic properties /." Full text open access at:, 2001. http://content.ohsu.edu/u?/etd,224.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Xie, Ning. "Caractérisation fonctionnelle des gènes de laccases et de bilirubine oxydases, appartenant à la famille des gènes multicopper oxydases, chez le champignon coprophile Podospora anserina : vers une meilleure compréhension de la dégradation de la lignocellulose par les champignons." Paris 7, 2014. http://www.theses.fr/2014PA077067.

Full text
Abstract:
L'amélioration de la transformation de la biomasse des plantes pour en faire des biocarburants est une étape importante pour le développement de nouvelles sources d'énergie propres et renouvelables. Les multicopper oxydases (MCOs), tout particulièrement les laccases, sont supposées être impliquées dans la lyse de la lignine, étape prérequise pour une dégradation efficace de la cellulose en sucres fermentables. Les laccases fongiques sont utilisées dans beaucoup d'applications biotechnologiques comme l'industrie textile, la bioremédiation et comme biosenseurs. Plus récemment, d'autres MCOs, les
APA, Harvard, Vancouver, ISO, and other styles
6

Claud, Philippe. "Implication de la Semicarbazide-Sensitive-Amine-Oxydase dans le métabolisme d'une nouvelle entité chimique." Dijon, 2001. http://www.theses.fr/2001DIJOPE05.

Full text
Abstract:
Le métabolisme du trespérimus, nouvel agent immunosuppresseur de la classe des polyamines, a été étudié chez l'homme et chez le rat. Le médicament est éliminé par un intense métabolisme non hépatique. Des études in vivo chez le rat et chez l'homme, combinant des analyses radio-HPLC et LC/MS, ont permis d'identifier deux voies de biotransformation. La principale voie métabolique du médicament concerne les désaminations oxydatives de sa moitié spermidine, particulièrement chez l'homme. L'autre route catabolique initiée par une réaction d'hydrolyse semble également impliquer une réaction de désam
APA, Harvard, Vancouver, ISO, and other styles
7

Braun, Julian F. W. [Verfasser]. "Regulation der Amine Oxidase Copper-containing 1 durch den Wilms-Tumor-Transkriptionsfaktor 1 / Julian F. W. Braun." Berlin : Medizinische Fakultät Charité - Universitätsmedizin Berlin, 2016. http://d-nb.info/1119803047/34.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Jakobsson, Emma. "Structural Studies of Echinococcus granulosus Fatty-acid-binding Protein 1 and Human Semicarbazide-sensitive Amine Oxidase." Doctoral thesis, Uppsala : Acta Universitatis Upsaliensis: Univ.-bibl. [distributör], 2005. http://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-5884.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

Groß, Felicitas Barbara [Verfasser], Jörg [Akademischer Betreuer] [Gutachter] Durner, and Erich [Gutachter] Glawischnig. "COPPER AMINE OXIDASE 8 (CuAO8) participates in the regulation of nitric oxide production during salt stress in seedlings of Arabidopsis thaliana / Felicitas Barbara Groß ; Gutachter: Jörg Durner, Erich Glawischnig ; Betreuer: Jörg Durner." München : Universitätsbibliothek der TU München, 2016. http://d-nb.info/112664417X/34.

Full text
APA, Harvard, Vancouver, ISO, and other styles

Books on the topic "Copper. Amine oxidase. Quinone"

1

1945-, Floris Giovanni, and Mondovì Bruno, eds. Copper amine oxidases: Structures, catalytic mechanisms, and role in pathophysiology. Taylor & Francis, 2009.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
2

Copper Amine Oxidases: Structure, Catalytic Mechanism and Role in Physiopathlology. CRC, 2009.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
3

Mondovi, Bruno, and Giovanni Floris. Copper Amine Oxidases: Structures, Catalytic Mechanisms and Role in Pathophysiology. Taylor & Francis Group, 2009.

Find full text
APA, Harvard, Vancouver, ISO, and other styles
4

Mondovi, Bruno, and Giovanni Floris. Copper Amine Oxidases: Structures, Catalytic Mechanisms and Role in Pathophysiology. Taylor & Francis Group, 2017.

Find full text
APA, Harvard, Vancouver, ISO, and other styles

Book chapters on the topic "Copper. Amine oxidase. Quinone"

1

Tanizawa, Katsuyuki, Hideyuki Matsunami, and Hiroshi Yamaguchi. "Mechanism of Topa Quinone Biogenesis in Copper Amine Oxidase Studied by Site-Directed Mutagenesis and X-Ray Crystallography." In Biochemistry and Molecular Biology of Vitamin B6 and PQQ-dependent Proteins. Birkhäuser Basel, 2000. http://dx.doi.org/10.1007/978-3-0348-8397-9_11.

Full text
APA, Harvard, Vancouver, ISO, and other styles
2

Klinman, Judith, and Albert Lang. "Copper Amine Oxidase." In Encyclopedia of Metalloproteins. Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-1533-6_335.

Full text
APA, Harvard, Vancouver, ISO, and other styles
3

Rokhsana, Dalia, Eric M. Shepard, Doreen E. Brown, and David M. Dooley. "Amine Oxidase and Galactose Oxidase." In Copper-Oxygen Chemistry. John Wiley & Sons, Inc., 2011. http://dx.doi.org/10.1002/9781118094365.ch3.

Full text
APA, Harvard, Vancouver, ISO, and other styles
4

Schomburg, Dietmar, Margit Salzmann, and Dörte Stephan. "Amine oxidase (copper-containing)." In Enzyme Handbook. Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-642-58051-2_171.

Full text
APA, Harvard, Vancouver, ISO, and other styles
5

Klinman, Judith P., Danying Cai, and Sophie Xuefei Wang. "Quinocofactors in Copper Amine Oxidases and Lysyl Oxidase." In Microbial Growth on C1 Compounds. Springer Netherlands, 1996. http://dx.doi.org/10.1007/978-94-009-0213-8_23.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

Angelini, Riccardo, Alessandra Cona, and Paraskevi Tavladoraki. "Determination of Copper Amine Oxidase Activity in Plant Tissues." In Methods in Molecular Biology. Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-7398-9_13.

Full text
APA, Harvard, Vancouver, ISO, and other styles
7

Rucker, Robert B., Changtai Cui, Eskouhie H. Tchaparian, et al. "Dietary Copper, Vanadate, Lysyl Oxidase Activity, and Lysine Tyrosyl Quinone Formation." In Trace Elements in Man and Animals 10. Springer US, 2002. http://dx.doi.org/10.1007/0-306-47466-2_292.

Full text
APA, Harvard, Vancouver, ISO, and other styles
8

Tanizawa, Katsuyuki, Ryuichi Matsuzaki, and Toshio Fukui. "Copper ion-dependent biogenesis of topa quinone cofactor covalently bound to bacterial monoamine oxidase." In Biochemistry of Vitamin B6 and PQQ. Birkhäuser Basel, 1994. http://dx.doi.org/10.1007/978-3-0348-7393-2_43.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

Suzuki, Shinnichiro, Takeshi Sakurai, Shinobu Itoh, and Yoshiki Ohshiro. "Copper(II) Complexes Containing Reduced PQQ as a Model for the active Site of Copper-Requiring Amine Oxidase." In PQQ and Quinoproteins. Springer Netherlands, 1989. http://dx.doi.org/10.1007/978-94-009-0957-1_38.

Full text
APA, Harvard, Vancouver, ISO, and other styles
10

Shoji, Tsubasa. "Analysis of the Intracellular Localization of Transiently Expressed and Fluorescently Labeled Copper-Containing Amine Oxidases, Diamine Oxidase and N-Methylputrescine Oxidase in Tobacco, Using an Agrobacterium Infiltration Protocol." In Methods in Molecular Biology. Springer New York, 2017. http://dx.doi.org/10.1007/978-1-4939-7398-9_20.

Full text
APA, Harvard, Vancouver, ISO, and other styles
You might also be interested in the extended bibliographies on the topic 'Copper. Amine oxidase. Quinone' for particular source types:
Journal articles
We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!

To the bibliography