Relevant bibliographies by topics / Metalloenzimi

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Metalloenzimi'

Author: Grafiati
Published: 9 March 2023
Last updated: 31 July 2025

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Journal articles on the topic "Metalloenzimi"

1

Höcker, Birte. "A metalloenzyme reloaded." Nature Chemical Biology 8, no. 3 (2012): 224–25. http://dx.doi.org/10.1038/nchembio.800.

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You, Jing-Song, Xiao-Qi Yu, Xiao-Yu Su, et al. "Hydrolytic metalloenzyme models." Journal of Molecular Catalysis A: Chemical 202, no. 1-2 (2003): 17–22. http://dx.doi.org/10.1016/s1381-1169(03)00199-7.

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Dong, Steven D., and Ronald Breslow. "Bifunctional cyclodextrin metalloenzyme mimics." Tetrahedron Letters 39, no. 51 (1998): 9343–46. http://dx.doi.org/10.1016/s0040-4039(98)02160-1.

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Hadianawala, Murtuza, and Bhaskar Datta. "Design and development of sulfonylurea derivatives as zinc metalloenzyme modulators." RSC Advances 6, no. 11 (2016): 8923–29. http://dx.doi.org/10.1039/c5ra27341b.

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Kwon, Hanna, Jaswir Basran, Juliette M. Devos, et al. "Visualizing the protons in a metalloenzyme electron proton transfer pathway." Proceedings of the National Academy of Sciences 117, no. 12 (2020): 6484–90. http://dx.doi.org/10.1073/pnas.1918936117.

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In redox metalloenzymes, the process of electron transfer often involves the concerted movement of a proton. These processes are referred to as proton-coupled electron transfer, and they underpin a wide variety of biological processes, including respiration, energy conversion, photosynthesis, and metalloenzyme catalysis. The mechanisms of proton delivery are incompletely understood, in part due to an absence of information on exact proton locations and hydrogen bonding structures in a bona fide metalloenzyme proton pathway. Here, we present a 2.1-Å neutron crystal structure of the complex form
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Valdez, Crystal E., Amanda Morgenstern, Mark E. Eberhart, and Anastassia N. Alexandrova. "Predictive methods for computational metalloenzyme redesign – a test case with carboxypeptidase A." Physical Chemistry Chemical Physics 18, no. 46 (2016): 31744–56. http://dx.doi.org/10.1039/c6cp02247b.

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Doerr, Allison. "Metalloenzyme structures in a shot." Nature Methods 10, no. 4 (2013): 287. http://dx.doi.org/10.1038/nmeth.2428.

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Lancaster, Kyle M. "Revving up an artificial metalloenzyme." Science 361, no. 6407 (2018): 1071–72. http://dx.doi.org/10.1126/science.aau7754.

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Stoecker, Walter, Russell L. Wolz, Robert Zwilling, Daniel J. Strydom, and David S. Auld. "Astacus protease, a zinc metalloenzyme." Biochemistry 27, no. 14 (1988): 5026–32. http://dx.doi.org/10.1021/bi00414a012.

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Vallee, B. L. "Zinc metalloenzyme structure and function." Journal of Inorganic Biochemistry 36, no. 3-4 (1989): 299. http://dx.doi.org/10.1016/0162-0134(89)84446-0.

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Dissertations / Theses on the topic "Metalloenzimi"

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ROVALETTI, ANNA. "A computational outlook on the catalysis exerted by the unique active site of MoCu CO dehydrogenases." Doctoral thesis, Università degli Studi di Milano-Bicocca, 2021. http://hdl.handle.net/10281/305403.

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I processi di produzione e consumo negli ecosistemi del suolo contribuiscono ai cicli biochimici globali di molti gas in tracce (CH4, CO, H2, N2O e NO) che sono rilevanti per la chimica atmosferica e il clima. Tali piccole molecole di gas svolgono ruoli diversi nel metabolismo dei microrganismi posti nel suolo che si basano su metalloenzimi specifici per la loro trasformazione. Tra questi, è stato dimostrato che i metalloenzimi a base di molibdeno sono cruciali in tale contesto. In particolare, è stato riportato che un molibdoenzima specifico è coinvolto nell'ossidazione della CO atmosferica.
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Kluge, Stefan. "Modellierung sequentieller Metalloenzyme auf Magnesiumbasis." lizenzfrei, 2007. http://www.db-thueringen.de/servlets/DocumentServlet?id=10371.

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Kung, Yan. "Structural studies of metalloenzyme complexes in acetogenic carbon fixation." Thesis, Massachusetts Institute of Technology, 2011. http://hdl.handle.net/1721.1/65474.

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Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Chemistry, 2011.<br>Vita. Cataloged from PDF version of thesis.<br>Includes bibliographical references.<br>Acetogenic bacteria use the Wood-Ljungdahl carbon fixation pathway to produce cellular carbon from CO₂. This process requires several metalloenzymes that employ transition metals such as iron, nickel, and cobalt towards the production of acetyl-CoA, the final product. In one stage of the pathway, the cobalt-containing B₁₂ cofactor harbored by the corrinoid iron-sulfur protein (CFeSP) transfers a methyl group from methyltetra
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Murray, Jill Isobel. "A metalloenzyme model for the biotransformation of nitroglycerin to nitric oxide." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2002. http://www.collectionscanada.ca/obj/s4/f2/dsk3/ftp05/MQ63344.pdf.

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Schweitzer, Dirk. "Biomimetic models of the active site of the metalloenzyme nitrile hydratase /." Thesis, Connect to this title online; UW restricted, 2001. http://hdl.handle.net/1773/8692.

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Neupane, Kosh Prasad. "Nickel superoxide dismutase insight into the metalloenzyme gained from functional metallopeptide models /." abstract and full text PDF (UNR users only), 2009. http://0-gateway.proquest.com.innopac.library.unr.edu/openurl?url_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:dissertation&res_dat=xri:pqdiss&rft_dat=xri:pqdiss:3355593.

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Keppetipola, Niroshika. "Characterization of DNA and RNA end modifying enzymes and a triphosphate tunnel metalloenzyme /." Access full-text from WCMC, 2009. http://proquest.umi.com/pqdweb?did=1619359881&sid=5&Fmt=2&clientId=8424&RQT=309&VName=PQD.

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Saysell, Colin G. "Reactivity of the copper containing enzyme galactose oxidase." Thesis, University of Newcastle Upon Tyne, 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.307890.

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Benini, Stefano. "Structure and function relationships of urease and cytochrome c-553 from Bacillus pasteurii." Thesis, University of York, 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.325599.

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Huang, Qiongying. "In Vitro Study of Two Virulence Factors of Listeria monocytogenes: Cytolysin LLO and Metalloenzyme PC-PLC." Thesis, Boston College, 2014. http://hdl.handle.net/2345/bc-ir:103619.

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Thesis advisor: Mary F. Roberts<br>Thesis advisor: Jianmin Gao<br>The research reported in this thesis focused on three proteinaceous virulence factors of the intracellular bacterial pathogen Listeria monocytogenes: listeriolysin O (LLO), broad-range phospholipase C (PC-PLC), and phosphatidylinositol-specific phospholipase C (PI-PLC). Based on sequence homology of LLO with other cholesterol-dependent cytolysins (CDC), the protein has four domains of which domain 4 is thought to anchor the protein to cholesterol-containing surfaces while domain 3 mediates protein-protein binding on the membrane
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Books on the topic "Metalloenzimi"

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Kaup, Yoka. Metalloenzyme in der molekularen Archäologie. [s.n.], 1997.

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Likhtenshtein, Gertz I. Chemical Physics of Redox Metalloenzyme Catalysis. Springer Berlin Heidelberg, 1988. http://dx.doi.org/10.1007/978-3-642-73100-6.

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I, Likhtenshteĭn G. Chemical physics of redox metalloenzyme catalysis. Springer-Verlag, 1988.

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4

Hanson, Graeme, and Lawrence Berliner, eds. Future Directions in Metalloprotein and Metalloenzyme Research. Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-59100-1.

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1943-, Reedijk Jan, and Bouwman Elisabeth 1963-, eds. Bioinorganic catalysis. 2nd ed. Marcel Dekker, Inc., 1999.

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F, Riordan James, and Vallee Bert L, eds. Metallobiochemistry. Academic Press, 1988.

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Likhtenshtein, Gertz I., and Artavaz Beknazarov. Chemical Physics of Redox Metalloenzyme Catalysis. Springer, 2011.

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8

Berliner, Lawrence, and Graeme Hanson. Future Directions in Metalloprotein and Metalloenzyme Research. Springer, 2018.

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Berliner, Lawrence, and Graeme Hanson. Future Directions in Metalloprotein and Metalloenzyme Research. Springer International Publishing AG, 2017.

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10

Brandt, Jeffrey J. The structural and kinetic characterization of VanX: A metalloenzyme conferring high-level vancomycin resistance. 2000.

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Book chapters on the topic "Metalloenzimi"

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Meißner, D., and T. Arndt. "Metalloenzyme." In Lexikon der Medizinischen Laboratoriumsdiagnostik. Springer Berlin Heidelberg, 2017. http://dx.doi.org/10.1007/978-3-662-49054-9_2110-1.

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Meißner, D., and T. Arndt. "Metalloenzyme." In Springer Reference Medizin. Springer Berlin Heidelberg, 2019. http://dx.doi.org/10.1007/978-3-662-48986-4_2110.

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Kimura, Eiichi, and Mitsuhiko Shionoya. "Macrocyclic Polyamine Complex Beyond Metalloenzyme Models." In Transition Metals in Supramolecular Chemistry. Springer Netherlands, 1994. http://dx.doi.org/10.1007/978-94-015-8380-0_13.

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Goldberg, David P., and Stephen J. Lippard. "Modeling Phenoxyl Radical Metalloenzyme Active Sites." In Advances in Chemistry. American Chemical Society, 1996. http://dx.doi.org/10.1021/ba-1995-0246.ch003.

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Hisaeda, Yoshio. "Electroorganic Synthesis Mediated by Metalloenzyme Models." In New Challenges in Organic Electrochemistry. CRC Press, 2024. http://dx.doi.org/10.1201/9781003580645-20.

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Likhtenshtein, Gertz I. "General Information on Metalloenzymes and Metal Carriers." In Chemical Physics of Redox Metalloenzyme Catalysis. Springer Berlin Heidelberg, 1988. http://dx.doi.org/10.1007/978-3-642-73100-6_1.

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Likhtenshtein, Gertz I. "Energy, Entropy and Molecular-Dynamic Relationships in Enzyme Catalysis." In Chemical Physics of Redox Metalloenzyme Catalysis. Springer Berlin Heidelberg, 1988. http://dx.doi.org/10.1007/978-3-642-73100-6_10.

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Likhtenshtein, Gertz I. "Mechanisms of the Elementary Acts of Redox and Coupled Processes Involving Metalloenzymes and Carriers." In Chemical Physics of Redox Metalloenzyme Catalysis. Springer Berlin Heidelberg, 1988. http://dx.doi.org/10.1007/978-3-642-73100-6_11.

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Likhtenshtein, Gertz I. "Physical Methods of Investigation of Metalloenzymes." In Chemical Physics of Redox Metalloenzyme Catalysis. Springer Berlin Heidelberg, 1988. http://dx.doi.org/10.1007/978-3-642-73100-6_2.

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Likhtenshtein, Gertz I. "Physical Label Techniques." In Chemical Physics of Redox Metalloenzyme Catalysis. Springer Berlin Heidelberg, 1988. http://dx.doi.org/10.1007/978-3-642-73100-6_3.

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Conference papers on the topic "Metalloenzimi"

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Collinsová, Michaela, Carmen Castro, Timothy Garrow, Vincent Dive, Athanasios Yiotakis, and Jiří Jiráček. "Development of novel inhibitors of Zn-metalloenzyme betaine: Homocysteine S-methyltransferase." In VIIth Conference Biologically Active Peptides. Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 2001. http://dx.doi.org/10.1135/css200104049.

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Born, Benjamin, Matthias Heyden, Moran Grossman, Irit Sagi, and Martina Havenith. "Protein-water network dynamics during metalloenzyme hydrolysis observed by kinetic THz absorption (KITA)." In SPIE BiOS, edited by Gerald J. Wilmink and Bennett L. Ibey. SPIE, 2013. http://dx.doi.org/10.1117/12.2000715.

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Kirby, Edward P., Mary Ann Mascelli, Carol Silverman, and Daniel W. Karl. "LOCALIZATION OF THE PLATELET-BINDING AND HEPARIN-BINDING DOMAINS OF BOVINE VON WILLEBRAND FACTOR." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644097.

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Bovine von Willebrand Factor (vWF) binds directly to human platelets and also to heparin-agarose. Cleavage of vWF with Protease I, a metalloenzyme isolated from the venom of the western diamondback rattlesnake, produces two major fragments with apparent Mr of 250 kD and 200 kD. The 200 kD fragment competes with native vWF for binding to the GPIb-associated vWF receptor on formalin-fixed human platelets and has weak platelet-agglutinating activity. It is composed of three polypeptide chains of apparent Mr of 97 kD, 61 kD, and 35 kD. Monoclonal antibodies #2 and H-9, which inhibit binding of vWF
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Reports on the topic "Metalloenzimi"

1

Balch, William. Purification and characterization of dihydroorotase from Clostridium oroticum, a zinc-containing metalloenzyme. Portland State University Library, 2000. http://dx.doi.org/10.15760/etd.1687.

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