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Journal articles on the topic 'Metalloenzymes'

Author: Grafiati

Published: 4 June 2021

Last updated: 26 July 2025

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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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2

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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3

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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4

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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5

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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6

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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7

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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8

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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9

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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10

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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11

Richichi, Barbara, Georgios A. Spyroulias, Jean-Yves Winum, and Raivis Žalubovskis. "Metalloenzymes as Therapeutic Targets." Current Medicinal Chemistry 26, no. 15 (2019): 2556–57. http://dx.doi.org/10.2174/092986732615190725122012.

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12

Zastrow, Melissa L., and Vincent L. Pecoraro. "Designing Hydrolytic Zinc Metalloenzymes." Biochemistry 53, no. 6 (2014): 957–78. http://dx.doi.org/10.1021/bi4016617.

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13

Drennan, C. "Surprising cofactors in metalloenzymes." Current Opinion in Structural Biology 13, no. 2 (2003): 220–26. http://dx.doi.org/10.1016/s0959-440x(03)00038-1.

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14

Thauer, R. "Metalloenzymes involved in methanogenesis." Journal of Inorganic Biochemistry 59, no. 2-3 (1995): 86. http://dx.doi.org/10.1016/0162-0134(95)97198-y.

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15

Hyman, Michael R., and Arp Daniel. "Acetylene inhibition of metalloenzymes." Analytical Biochemistry 173, no. 2 (1988): 207–20. http://dx.doi.org/10.1016/0003-2697(88)90181-9.

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16

Esposito, Emilio Xavier, Kelli Baran, Ken Kelly, and Jeffry D. Madura. "Docking Substrates to Metalloenzymes." Molecular Simulation 24, no. 4-6 (2000): 293–306. http://dx.doi.org/10.1080/08927020008022377.

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17

Ueno, Takafumi. "Special Issue: Artificial Metalloenzymes." Israel Journal of Chemistry 55, no. 1 (2015): 13. http://dx.doi.org/10.1002/ijch.201410018.

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18

Thomas, Christophe M., and Thomas R. Ward. "Design of artificial metalloenzymes." Applied Organometallic Chemistry 19, no. 1 (2005): 35–39. http://dx.doi.org/10.1002/aoc.726.

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19

Rosati, Fiora, and Gerard Roelfes. "ChemInform Abstract: Artificial Metalloenzymes." ChemInform 41, no. 47 (2010): no. http://dx.doi.org/10.1002/chin.201047240.

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20

Casella, Luigi. "METALLOENZYMES AND CHEMICAL BIOMIMETICS." European Journal of Inorganic Chemistry 2006, no. 18 (2006): 3545–46. http://dx.doi.org/10.1002/ejic.200690036.

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21

Ebensperger, Paul, and Claudia Jessen-Trefzer. "Artificial metalloenzymes in a nutshell: the quartet for efficient catalysis." Biological Chemistry 403, no. 4 (2021): 403–12. http://dx.doi.org/10.1515/hsz-2021-0329.

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Abstract Artificial metalloenzymes combine the inherent reactivity of transition metal catalysis with the sophisticated reaction control of natural enzymes. By providing new opportunities in bioorthogonal chemistry and biocatalysis, artificial metalloenzymes have the potential to overcome certain limitations in both drug discovery and green chemistry or related research fields. Ongoing advances in organometallic catalysis, directed evolution, and bioinformatics are enabling the design of increasingly powerful systems that outperform conventional catalysis in a growing number of cases. Therefor

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22

Moianos, Dimitrios, Georgia-Myrto Prifti, Maria Makri, and Grigoris Zoidis. "Targeting Metalloenzymes: The “Achilles’ Heel” of Viruses and Parasites." Pharmaceuticals 16, no. 6 (2023): 901. http://dx.doi.org/10.3390/ph16060901.

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Metalloenzymes are central to the regulation of a wide range of essential viral and parasitic functions, including protein degradation, nucleic acid modification, and many others. Given the impact of infectious diseases on human health, inhibiting metalloenzymes offers an attractive approach to disease therapy. Metal-chelating agents have been expansively studied as antivirals and antiparasitics, resulting in important classes of metal-dependent enzyme inhibitors. This review provides the recent advances in targeting the metalloenzymes of viruses and parasites that impose a significant burden

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23

Di Leo, Riccardo, Doretta Cuffaro, Armando Rossello, and Elisa Nuti. "Bacterial Zinc Metalloenzyme Inhibitors: Recent Advances and Future Perspectives." Molecules 28, no. 11 (2023): 4378. http://dx.doi.org/10.3390/molecules28114378.

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Human deaths caused by Gram-negative bacteria keep rising due to the multidrug resistance (MDR) phenomenon. Therefore, it is a priority to develop novel antibiotics with different mechanisms of action. Several bacterial zinc metalloenzymes are becoming attractive targets since they do not show any similarities with the human endogenous zinc-metalloproteinases. In the last decades, there has been an increasing interest from both industry and academia in developing new inhibitors against those enzymes involved in lipid A biosynthesis, and bacteria nutrition and sporulation, e.g., UDP-[3-O-(R)-3-

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24

Kato, Masaru. "(Invited) Protein Film Electrochemistry and Surface-Enhanced Infrared Absorption Spectroscopy of Transmembrane Metalloenzymes." ECS Meeting Abstracts MA2024-02, no. 54 (2024): 3670. https://doi.org/10.1149/ma2024-02543670mtgabs.

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Transmembrane metalloenzymes encapsulating transition metal complexes are involved in electron transfer and in material transformation in living organisms. Understanding their operating principles is not only important for identifying the origin of highly efficient enzymatic reactions but also for developing sensors and catalysts inspired by metalloenzymes [1]. Protein film electrochemistry (PFE) is a powerful technique to investigate the redox behavior and enzymatic activity of transmembrane metalloenzymes even with a submonolayer amount of the target protein (~10 pmol cm–2). The challenge of

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25

Avenier, Fréderic, Wadih Ghattas, Rémy Ricoux, and Jean‐Pierre Mahy. "Recent progress in the development of new artificial metalloenzymes as biocatalysts for selective oxidations and Diels‐Alder reaction ‐ Mini‐Review." Vietnam Journal of Chemistry 58, no. 4 (2020): 423–33. http://dx.doi.org/10.1002/vjch.202000033.

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AbstractOur recent research is turning towards the elaboration of artificial metalloenzymes that catalyze reactions of interest for organic chemistry under eco‐compatible conditions. First, totally artificial metalloenzymes that catalyze selective oxidations in water are described following three main lines: (i) Insertion of microperoxidase 8 into Metal Organic Frameworks leading to artificial metalloenzymes as new biocatalysts for the selective sulfoxydation of sulfides and oxidation of dyes and by H2O2; (ii) Design of a new polyimine polymer‐based artificial reductase that allows the reducti

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26

Žalubovskis, Raivis, and Jean-Yves Winum. "Inhibitors of Selected Bacterial Metalloenzymes." Current Medicinal Chemistry 26, no. 15 (2019): 2690–714. http://dx.doi.org/10.2174/0929867325666180403154018.

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The utilization of bacterial metalloenzymes, especially ones not having mammalian (human) counterparts, has drawn attention to develop novel antibacterial agents to overcome drug resistance and especially multidrug resistance. In this review, we focus on the recent achievements on the development of inhibitors of bacterial enzymes peptide deformylase (PDF), metallo-&#946;-lactamase (MBL), methionine aminopeptidase (MetAP) and UDP-3-O-acyl- N-acetylglucosamine deacetylase (LpxC). The state of the art of the design and investigation of inhibitors of bacterial metalloenzymes is presented, and

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27

Chen, Allie Y., Rebecca N. Adamek, Benjamin L. Dick, Cy V. Credille, Christine N. Morrison, and Seth M. Cohen. "Targeting Metalloenzymes for Therapeutic Intervention." Chemical Reviews 119, no. 2 (2018): 1323–455. http://dx.doi.org/10.1021/acs.chemrev.8b00201.

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28

Davis, Holly J., and Thomas R. Ward. "Artificial Metalloenzymes: Challenges and Opportunities." ACS Central Science 5, no. 7 (2019): 1120–36. http://dx.doi.org/10.1021/acscentsci.9b00397.

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29

Valdez, Crystal E., Quentin A. Smith, Michael R. Nechay, and Anastassia N. Alexandrova. "Mysteries of Metals in Metalloenzymes." Accounts of Chemical Research 47, no. 10 (2014): 3110–17. http://dx.doi.org/10.1021/ar500227u.

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30

Yu, Fangting, Virginia M. Cangelosi, Melissa L. Zastrow, et al. "Protein Design: Toward Functional Metalloenzymes." Chemical Reviews 114, no. 7 (2014): 3495–578. http://dx.doi.org/10.1021/cr400458x.

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31

Bos, Jeffrey, and Gerard Roelfes. "Artificial metalloenzymes for enantioselective catalysis." Current Opinion in Chemical Biology 19 (April 2014): 135–43. http://dx.doi.org/10.1016/j.cbpa.2014.02.002.

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32

Tavares, P., A. S. Pereira, J. J. G. Moura, and I. Moura. "Metalloenzymes of the denitrification pathway." Journal of Inorganic Biochemistry 100, no. 12 (2006): 2087–100. http://dx.doi.org/10.1016/j.jinorgbio.2006.09.003.

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33

Benson, D. E., M. S. Wisz, and H. W. Hellinga. "Rational design of nascent metalloenzymes." Proceedings of the National Academy of Sciences 97, no. 12 (2000): 6292–97. http://dx.doi.org/10.1073/pnas.97.12.6292.

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34

Ilie, Adriana, and Manfred T. Reetz. "Directed Evolution of Artificial Metalloenzymes." Israel Journal of Chemistry 55, no. 1 (2014): 51–60. http://dx.doi.org/10.1002/ijch.201400087.

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35

Buettner, Katherine, Sarah Marcus, Raphael Rudatsikira, Savarna Goutam, and Amanda Reig. "Abstract 2339 Hydrolytic mini-metalloenzymes." Journal of Biological Chemistry 301, no. 5 (2025): 109988. https://doi.org/10.1016/j.jbc.2025.109988.

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36

Hartwig, John F., and Thomas R. Ward. "New “Cats” in the House: Chemistry Meets Biology in Artificial Metalloenzymes and Repurposed Metalloenzymes." Accounts of Chemical Research 52, no. 5 (2019): 1145. http://dx.doi.org/10.1021/acs.accounts.9b00154.

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37

Maiti, Biplab K., and José J. G. Moura. "Native Protein Template Assisted Synthesis of Non-Native Metal-Sulfur Clusters." BioChem 2, no. 3 (2022): 182–97. http://dx.doi.org/10.3390/biochem2030013.

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Metalloenzymes are the most proficient nature catalysts that are responsible for diverse biochemical transformations introducing excellent selectivity and performing at high rates, using intricate mutual relationships between metal ions and proteins. Inspired by nature, chemists started using naturally occurring proteins as templates to harbor non-native metal catalysts for the sustainable synthesis of molecules for pharmaceutical, biotechnological and industrial purposes. Therefore, metalloenzymes are the relevant targets for the design of artificial biocatalysts. The search and development o

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38

Lin, Ying-Wu. "Rational Design of Artificial Metalloproteins and Metalloenzymes with Metal Clusters." Molecules 24, no. 15 (2019): 2743. http://dx.doi.org/10.3390/molecules24152743.

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Metalloproteins and metalloenzymes play important roles in biological systems by using the limited metal ions, complexes, and clusters that are associated with the protein matrix. The design of artificial metalloproteins and metalloenzymes not only reveals the structure and function relationship of natural proteins, but also enables the synthesis of artificial proteins and enzymes with improved properties and functions. Acknowledging the progress in rational design from single to multiple active sites, this review focuses on recent achievements in the design of artificial metalloproteins and m

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39

Feng, Haisong, Xuan Guo, Hui Zhang, et al. "Mechanistic insights into artificial metalloenzymes towards imine reduction." Physical Chemistry Chemical Physics 21, no. 42 (2019): 23408–17. http://dx.doi.org/10.1039/c9cp04473f.

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40

Horch, M., P. Hildebrandt, and I. Zebger. "Concepts in bio-molecular spectroscopy: vibrational case studies on metalloenzymes." Physical Chemistry Chemical Physics 17, no. 28 (2015): 18222–37. http://dx.doi.org/10.1039/c5cp02447a.

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41

Horch, Marius. "Rational redox tuning of transition metal sites: learning from superoxide reductase." Chemical Communications 55, no. 62 (2019): 9148–51. http://dx.doi.org/10.1039/c9cc04004h.

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42

JOHNSON, M. K. "Metalloenzymes: The Bioinorganic Chemistry of Nickel." Science 244, no. 4904 (1989): 591. http://dx.doi.org/10.1126/science.244.4904.591.

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43

McCall, Keith A., Chih-chin Huang, and Carol A. Fierke. "Function and Mechanism of Zinc Metalloenzymes." Journal of Nutrition 130, no. 5 (2000): 1437S—1446S. http://dx.doi.org/10.1093/jn/130.5.1437s.

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44

Karlin, K. "Metalloenzymes, structural motifs, and inorganic models." Science 261, no. 5122 (1993): 701–8. http://dx.doi.org/10.1126/science.7688141.

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45

Pyle, A. "Ribozymes: a distinct class of metalloenzymes." Science 261, no. 5122 (1993): 709–14. http://dx.doi.org/10.1126/science.7688142.

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46

Nam, Wonwoo. "Dioxygen Activation by Metalloenzymes and Models." Accounts of Chemical Research 40, no. 7 (2007): 465. http://dx.doi.org/10.1021/ar700131d.

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47

Jaffe, Eileen K. "The porphobilinogen synthase family of metalloenzymes." Acta Crystallographica Section D Biological Crystallography 56, no. 2 (2000): 115–28. http://dx.doi.org/10.1107/s0907444999014894.

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48

Lovell, T. "Density functional methods applied to metalloenzymes." Coordination Chemistry Reviews 238-239 (March 2003): 211–32. http://dx.doi.org/10.1016/s0010-8545(02)00331-4.

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49

White, R. "Targeting metalloenzymes: a strategy that works." Current Opinion in Pharmacology 3, no. 5 (2003): 502–7. http://dx.doi.org/10.1016/s1471-4892(03)00115-2.

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50

Khandelwal, S., D. N. Kachru, and S. K. Tandon. "Influence of metal chelators on metalloenzymes." Toxicology Letters 37, no. 3 (1987): 213–19. http://dx.doi.org/10.1016/0378-4274(87)90134-2.

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