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Relevant bibliographies by topics / Metalloenzymes

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Academic literature on the topic 'Metalloenzymes'

Author: Grafiati

Published: 4 June 2021

Last updated: 26 July 2025

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Journal articles on the topic "Metalloenzymes"

1

Zhang, Lu, Yajun Yang, Ying Yang, and Zhiyan Xiao. "Discovery of Novel Metalloenzyme Inhibitors Based on Property Characterization: Strategy and Application for HDAC1 Inhibitors." Molecules 29, no. 5 (2024): 1096. http://dx.doi.org/10.3390/molecules29051096.

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Metalloenzymes are ubiquitously present in the human body and are relevant to a variety of diseases. However, the development of metalloenzyme inhibitors is limited by low specificity and poor drug-likeness associated with metal-binding fragments (MBFs). A generalized drug discovery strategy was established, which is characterized by the property characterization of zinc-dependent metalloenzyme inhibitors (ZnMIs). Fifteen potential Zn2+-binding fragments (ZnBFs) were identified, and a customized pharmacophore feature was defined based on these ZnBFs. The customized feature was set as a require

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Gao, Liang, Ya Zhang, Lina Zhao, et al. "An artificial metalloenzyme for catalytic cancer-specific DNA cleavage and operando imaging." Science Advances 6, no. 29 (2020): eabb1421. http://dx.doi.org/10.1126/sciadv.abb1421.

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Metalloenzymes are promising anticancer candidates to overcome chemoresistance by involving unique mechanisms. To date, it is still a great challenge to obtain synthetic metalloenzymes with persistent catalytic performance for cancer-specific DNA cleavage and operando imaging. Here, an artificial metalloenzyme, copper cluster firmly anchored in bovine serum albumin conjugated with tumor-targeting peptide, is exquisitely constructed. It is capable of persistently transforming hydrogen peroxide in tumor microenvironment to hydroxyl radical and oxygen in a catalytic manner. The stable catalysis r

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Blanquart, Christophe, Camille Linot, Pierre-François Cartron, Daniela Tomaselli, Antonello Mai, and Philippe Bertrand. "Epigenetic Metalloenzymes." Current Medicinal Chemistry 26, no. 15 (2019): 2748–85. http://dx.doi.org/10.2174/0929867325666180706105903.

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Epigenetics controls the expression of genes and is responsible for cellular phenotypes. The fundamental basis of these mechanisms involves in part the post-translational modifications (PTMs) of DNA and proteins, in particular, the nuclear histones. DNA can be methylated or demethylated on cytosine. Histones are marked by several modifications including acetylation and/or methylation, and of particular importance are the covalent modifications of lysine. There exists a balance between addition and removal of these PTMs, leading to three groups of enzymes involved in these processes: the writer

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Rosati, Fiora, and Gerard Roelfes. "Artificial Metalloenzymes." ChemCatChem 2, no. 8 (2010): 916–27. http://dx.doi.org/10.1002/cctc.201000011.

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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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Cohen, Aina. "New Opportunities to Study Metalloprotein Structure and Dynamics." Structural Dynamics 12, no. 2_Supplement (2025): A320. https://doi.org/10.1063/4.0000626.

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Metalloenzymes play essential roles in nearly all biological processes and as such represent a rich target space for drug development and biomanufacturing. This presentation will address many of the challenges faced by crystallographers studying metalloproteins, including verification of the correct incorporation and chemical state of the metal of interest, and maintenance of the optimal environment for data collection, including anaerobic, aphotic, controlled humidity and/or temperature. Further, the metal centers of metalloenzymes, especially those that are redox active, are very susceptible

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Hoffman, Brian M. "ENDOR of Metalloenzymes." Accounts of Chemical Research 36, no. 7 (2003): 522–29. http://dx.doi.org/10.1021/ar0202565.

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Boer, Jodi L., Scott B. Mulrooney, and Robert P. Hausinger. "Nickel-dependent metalloenzymes." Archives of Biochemistry and Biophysics 544 (February 2014): 142–52. http://dx.doi.org/10.1016/j.abb.2013.09.002.

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Cheng, Yunqi, and Hongping Chen. "Aberrance of Zinc Metalloenzymes-Induced Human Diseases and Its Potential Mechanisms." Nutrients 13, no. 12 (2021): 4456. http://dx.doi.org/10.3390/nu13124456.

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Zinc, an essential micronutrient in the human body, is a component in over 300 enzymes and participates in regulating enzymatic activity. Zinc metalloenzymes play a crucial role in physiological processes including antioxidant, anti-inflammatory, and immune responses, as well as apoptosis. Aberrant enzyme activity can lead to various human diseases. In this review, we summarize zinc homeostasis, the roles of zinc in zinc metalloenzymes, the physiological processes of zinc metalloenzymes, and aberrant zinc metalloenzymes in human diseases. In addition, potential mechanisms of action are also di

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Sugrue, Elena, Carol J. Hartley, Colin Scott, and Colin J. Jackson. "The Evolution of New Catalytic Mechanisms for Xenobiotic Hydrolysis in Bacterial Metalloenzymes." Australian Journal of Chemistry 69, no. 12 (2016): 1383. http://dx.doi.org/10.1071/ch16426.

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An increasing number of bacterial metalloenzymes have been shown to catalyse the breakdown of xenobiotics in the environment, while others exhibit a variety of promiscuous xenobiotic-degrading activities. Several different evolutionary processes have allowed these enzymes to gain or enhance xenobiotic-degrading activity. In this review, we have surveyed the range of xenobiotic-degrading metalloenzymes, and discuss the molecular and catalytic basis for the development of new activities. We also highlight how our increased understanding of the natural evolution of xenobiotic-degrading metalloenz

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Dissertations / Theses on the topic "Metalloenzymes"

1

Wilkinson, Kay W. "Structural studies on metalloenzymes." Thesis, University of Sheffield, 1995. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.364295.

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Obrecht, Lorenz. "Artificial metalloenzymes in catalysis." Thesis, University of St Andrews, 2015. http://hdl.handle.net/10023/7248.

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This thesis describes the synthesis, characterisation and application of artificial metalloenzymes as catalysts. The focus was on two mutants of SCP-2L (SCP-2L A100C and SCP-2L V83C) both of which possess a hydrophobic tunnel in which apolar substrates can accumulate. The crystal structure of SCP-2L A100C was determined and discussed with a special emphasis on its hydrophobic tunnel. The SCP-2L mutants were covalently modified at their unique cysteine with two different N-ligands (phenanthroline or dipicolylamine based) or three different phosphine ligands (all based on triphenylphosphine) in

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Alonso, Cotchico Lur. "Computational design of artificial metalloenzymes." Doctoral thesis, Universitat Autònoma de Barcelona, 2018. http://hdl.handle.net/10803/664006.

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El diseño enzimático es el área basada en el descubrimiento y/o optimización de biomoléculas para el desarrollo de reacciones químicas no naturales. Es un área que se encuentra en su mayor crecimiento y constituye uno de los puntos clave en la transición de la química hacia alternativas más ecológicas. Una manera elegante de sintetizar nuevos biocatalizadores es mediante la inclusión de cofactores organometálicos en estructuras biológicas, dando lugar a lo que se conoce como Metaloenzimas Artificiales (ArMs). Estos híbridos combinan la versatilidad catalítica de los compuestos organometálicos

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Jackson, Henry Lee. "Synthetic models of Fe-type nitrile hydratase /." Thesis, Connect to this title online; UW restricted, 2002. http://hdl.handle.net/1773/8532.

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Dharmawardena, Priyangi Tikiri Kumari. "Artificial hydrolytic metalloenzymes for ester hydrolysis." Thesis, King's College London (University of London), 2000. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.322705.

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Woollard-Shore, John. "Towards functional models of copper metalloenzymes." Thesis, University of Essex, 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.364506.

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Pinkham, Andrew M. "Oxidative Biocatalysis in Metallotherapeutics and Metalloenzymes." The Ohio State University, 2018. http://rave.ohiolink.edu/etdc/view?acc_num=osu1534720716721343.

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Oshige, Eric Stephen. "Photorelease of caged alcohols from artificial metalloenzymes /." Electronic thesis, 2007. http://etd.wfu.edu/theses/available/etd-06102007-193011/.

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Hexter, Suzannah Victoria. "Principles of electrocatalysis by hydrogen activating metalloenzymes." Thesis, University of Oxford, 2014. http://ora.ox.ac.uk/objects/uuid:60aeee02-a16c-4c86-bf48-61306512fa86.

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Hydrogenases catalyse the interconversion of H<sub>2</sub> and H<sup>+</sup>. Protein Film Electrochemistry (PFE), a technique in which a redox enzyme is adsorbed directly onto an electrode, enables a detailed description of the catalytic function of these metalloenzymes to be obtained. Unlike small-molecule electrocatalysts, the hydrogenase active site is surrounded by a protein structure ensuring that it is relatively unperturbed by the electrode surface. In this thesis, PFE is used alongside mathematical modelling to explain diﬀerences between [NiFe]- and [FeFe]-hydrogenases, highlighting s

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Dutta, Rinku. "Detection of Metalloenzymes Employing Fluorescentpolymers and Liposomes." Diss., North Dakota State University, 2012. https://hdl.handle.net/10365/26636.

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In the biological systems, proteins are important constituents. Protein-protein interactions play vital roles in physiological environments and any disruption in these interactions lead to adverse effects. However, designing artificial receptor molecules or scaffolds to imitate or replace these endogenous partners could be an avenue for better drug designing and detection tools creation. We are primarily interested in polymer and liposomal systems to detect two crucial metalloenzymes of the living world. Matrix metalloproteinases are zinc-containing endopeptidases which are required for wound

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Books on the topic "Metalloenzymes"

1

Moura, Isabel, José J. G. Moura, Sofia R. Pauleta, and Luisa B. Maia, eds. Metalloenzymes in Denitrification. Royal Society of Chemistry, 2016. http://dx.doi.org/10.1039/9781782623762.

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Montserrat, Diéguez, Bäckvall Jan-E⋅, and Pàmies Oscar. Artificial Metalloenzymes and MetalloDNAzymes in Catalysis. Wiley-VCH Verlag GmbH & Co. KGaA, 2018. http://dx.doi.org/10.1002/9783527804085.

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Sei, Otsuka, and Yamanaka Tateo 1932-, eds. Metalloproteins: Chemical properties and biological effects. Kodansha Ltd., 1988.

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4

Bachmeier, Andreas S. J. L. Metalloenzymes as Inspirational Electrocatalysts for Artificial Photosynthesis. Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-47069-6.

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M, Harrison Pauline, ed. Metalloproteins. Verlag Chemie, 1985.

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6

Helmut, Sigel, and Sigel Astrid, eds. Metalloenzymes involving amino acid-residue and related radicals. M. Dekker, 1994.

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

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8

Helmut, Sigel, and Sigel Astrid, eds. Degradation of environmental pollutants by microorganisms and their metalloenzymes. M. Dekker, 1992.

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9

Hanson, Graeme Richard. High resolution EPR: Applications to metalloenzymes and metals in medicine. Springer, 2009.

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10

Hanson, Graeme. Metals in Biology: Applications of High-Resolution EPR to Metalloenzymes. Springer Science+Business Media, LLC, 2010.

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Book chapters on the topic "Metalloenzymes"

1

Hoppert, Michael. "Metalloenzymes." In Encyclopedia of Geobiology. Springer Netherlands, 2011. http://dx.doi.org/10.1007/978-1-4020-9212-1_134.

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Trindler, Christian, та Thomas R. Ward. "Artificial Metalloenzymes". У Effects of Nanoconﬁnement on Catalysis. Springer International Publishing, 2017. http://dx.doi.org/10.1007/978-3-319-50207-6_3.

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3

Chin, Jik, Mariusz Banaszczyk, Vrej Jubian, Jung Hee Kim, and Karen Mrejen. "Artificial Hydrolytic Metalloenzymes." In Bioorganic Chemistry Frontiers. Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-76241-3_5.

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Chin, Jik, and Hae-Jo Kim. "Artificial Hydrolytic Metalloenzymes." In Artificial Enzymes. Wiley-VCH Verlag GmbH & Co. KGaA, 2006. http://dx.doi.org/10.1002/3527606645.ch6.

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Harnden, Kevin A., Yajie Wang, Lam Vo, Huimin Zhao, and Yi Lu. "Engineering Artificial Metalloenzymes." In Protein Engineering. WILEY-VCH GmbH, 2021. http://dx.doi.org/10.1002/9783527815128.ch8.

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Klebe, Gerhard. "Inhibitors of Hydrolyzing Metalloenzymes." In Drug Design. Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-17907-5_25.

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Lewis, Jared C., and Ken Ellis-Guardiola. "Preparation of Artificial Metalloenzymes." In Artificial Metalloenzymes and MetalloDNAzymes in Catalysis. Wiley-VCH Verlag GmbH & Co. KGaA, 2018. http://dx.doi.org/10.1002/9783527804085.ch1.

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Borowski, Tomasz, and Maciej Szaleniec. "Challenges in Modelling Metalloenzymes." In Transition Metals in Coordination Environments. Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-11714-6_17.

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Galdes, Alphonse, and Bert L. Vallee. "Categories of Zinc Metalloenzymes." In Metal Ions in Biological Systems. CRC Press, 2023. http://dx.doi.org/10.1201/9781003418092-1.

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Jha, Srishti, Abdul Arif Khan, and Mohd Tashfeen Ashraf. "Designing of Artificial Metalloenzymes." In Biocatalysis. Springer International Publishing, 2019. http://dx.doi.org/10.1007/978-3-030-25023-2_9.

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Conference papers on the topic "Metalloenzymes"

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Yamaguchi, K., M. Shoji, T. Saito, et al. "Theory of chemical bonds in metalloenzymes - Manganese oxides clusters in the oxygen evolution center -." In INTERNATIONAL CONFERENCE OF COMPUTATIONAL METHODS IN SCIENCES AND ENGINEERING 2009: (ICCMSE 2009). AIP, 2012. http://dx.doi.org/10.1063/1.4771704.

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Opanike, Oyetunde, Olugbenga A. Omotosho, Emmanuel O. Akindele, and Omolola O. Yusuf. "Hepatocellular Effect of Copper Poisoning on the Liver and Kidney of Albino Rats (<i>Rattus norvicus</i>)." In 2023 International Conference on Sustainable Engineering and Materials Development. Trans Tech Publications Ltd, 2024. http://dx.doi.org/10.4028/p-vzg5cj.

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Copper and its salt are remarkably non-toxic to mammalian tissue. It is possible to ingest a large number of soluble copper salts such as copper sulphide to produce intoxication, nausea, vomiting, diarrhoea, and abdominal cramp. Copper salts are widely employed in agriculture and veterinary practice. Copper is an essential trace element in life and is a component of several metalloenzymes and other proteins such as cytochrome oxidase, heamocyanin, lysin oxidase, ascorbate oxidase and amine oxidase. When copper is present in the body above a particular dosage of greater than 100ppm in rats, it

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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 "Metalloenzymes"

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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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