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Journal articles on the topic 'Metalloenzimi'

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Author: Grafiati

Published: 9 March 2023

Last updated: 10 March 2023

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1

Höcker, Birte. "A metalloenzyme reloaded." Nature Chemical Biology 8, no. 3 (February 15, 2012): 224–25. http://dx.doi.org/10.1038/nchembio.800.

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2

You, Jing-Song, Xiao-Qi Yu, Xiao-Yu Su, Tao Wang, Qing-Xiang Xiang, Meng Yang, and Ru-Gang Xie. "Hydrolytic metalloenzyme models." Journal of Molecular Catalysis A: Chemical 202, no. 1-2 (August 2003): 17–22. http://dx.doi.org/10.1016/s1381-1169(03)00199-7.

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3

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

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4

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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5

Kwon, Hanna, Jaswir Basran, Juliette M. Devos, Reynier Suardíaz, Marc W. van der Kamp, Adrian J. Mulholland, Tobias E. Schrader, et al. "Visualizing the protons in a metalloenzyme electron proton transfer pathway." Proceedings of the National Academy of Sciences 117, no. 12 (March 9, 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 formed between a redox metalloenzyme (ascorbate peroxidase) and its reducing substrate (ascorbate). In the neutron structure of the complex, the protonation states of the electron/proton donor (ascorbate) and all of the residues involved in the electron/proton transfer pathway are directly observed. This information sheds light on possible proton movements during heme-catalyzed oxygen activation, as well as on ascorbate oxidation.

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6

Doerr, Allison. "Metalloenzyme structures in a shot." Nature Methods 10, no. 4 (March 28, 2013): 287. http://dx.doi.org/10.1038/nmeth.2428.

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7

Lancaster, Kyle M. "Revving up an artificial metalloenzyme." Science 361, no. 6407 (September 13, 2018): 1071–72. http://dx.doi.org/10.1126/science.aau7754.

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8

Stoecker, Walter, Russell L. Wolz, Robert Zwilling, Daniel J. Strydom, and David S. Auld. "Astacus protease, a zinc metalloenzyme." Biochemistry 27, no. 14 (July 12, 1988): 5026–32. http://dx.doi.org/10.1021/bi00414a012.

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9

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

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10

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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11

Jackl, Moritz K., Hyeonglim Seo, Johannes Karges, Mark Kalaj, and Seth M. Cohen. "Salicylate metal-binding isosteres as fragments for metalloenzyme inhibition." Chemical Science 13, no. 7 (2022): 2128–36. http://dx.doi.org/10.1039/d1sc06011b.

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12

Ehudin, Melanie A., Andrew W. Schaefer, Suzanne M. Adam, David A. Quist, Daniel E. Diaz, Joel A. Tang, Edward I. Solomon, and Kenneth D. Karlin. "Influence of intramolecular secondary sphere hydrogen-bonding interactions on cytochrome c oxidase inspired low-spin heme–peroxo–copper complexes." Chemical Science 10, no. 10 (2019): 2893–905. http://dx.doi.org/10.1039/c8sc05165h.

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13

Li, Yinghao, Mingpan Cheng, Jingya Hao, Changhao Wang, Guoqing Jia, and Can Li. "Terpyridine–Cu(ii) targeting human telomeric DNA to produce highly stereospecific G-quadruplex DNA metalloenzyme." Chemical Science 6, no. 10 (2015): 5578–85. http://dx.doi.org/10.1039/c5sc01381j.

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14

Schneider, Camille R., and Hannah S. Shafaat. "An internal electron reservoir enhances catalytic CO2 reduction by a semisynthetic enzyme." Chemical Communications 52, no. 64 (2016): 9889–92. http://dx.doi.org/10.1039/c6cc03901d.

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15

Johnson, Heather C., Shaoguang Zhang, Anna Fryszkowska, Serge Ruccolo, Sandra A. Robaire, Artis Klapars, Niki R. Patel, Aaron M. Whittaker, Mark A. Huffman, and Neil A. Strotman. "Biocatalytic oxidation of alcohols using galactose oxidase and a manganese(iii) activator for the synthesis of islatravir." Organic & Biomolecular Chemistry 19, no. 7 (2021): 1620–25. http://dx.doi.org/10.1039/d0ob02395g.

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16

Smith, Meghan A., Sean H. Majer, Avery C. Vilbert, and Kyle M. Lancaster. "Controlling a burn: outer-sphere gating of hydroxylamine oxidation by a distal base in cytochrome P460." Chemical Science 10, no. 13 (2019): 3756–64. http://dx.doi.org/10.1039/c9sc00195f.

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17

Reed, Christopher J., Quan N. Lam, Evan N. Mirts, and Yi Lu. "Molecular understanding of heteronuclear active sites in heme–copper oxidases, nitric oxide reductases, and sulfite reductases through biomimetic modelling." Chemical Society Reviews 50, no. 4 (2021): 2486–539. http://dx.doi.org/10.1039/d0cs01297a.

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18

Zubi, Yasmine S., Bingqing Liu, Yifan Gu, Dipankar Sahoo, and Jared C. Lewis. "Controlling the optical and catalytic properties of artificial metalloenzyme photocatalysts using chemogenetic engineering." Chemical Science 13, no. 5 (2022): 1459–68. http://dx.doi.org/10.1039/d1sc05792h.

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19

TAGAKI, Waichiro, and Kenji OGINO. "Proteolytic Metalloenzyme Models in Micellar Systems." Journal of Japan Oil Chemists' Society 39, no. 10 (1990): 744–52. http://dx.doi.org/10.5650/jos1956.39.10_744.

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20

Mayer, Clemens, Dennis G. Gillingham, Thomas R. Ward, and Donald Hilvert. "An artificial metalloenzyme for olefin metathesis." Chemical Communications 47, no. 44 (2011): 12068. http://dx.doi.org/10.1039/c1cc15005g.

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21

Bersellini, Manuela, and Gerard Roelfes. "A metal ion regulated artificial metalloenzyme." Dalton Transactions 46, no. 13 (2017): 4325–30. http://dx.doi.org/10.1039/c7dt00533d.

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22

Day, Joshua A., and Seth M. Cohen. "Investigating the Selectivity of Metalloenzyme Inhibitors." Journal of Medicinal Chemistry 56, no. 20 (October 14, 2013): 7997–8007. http://dx.doi.org/10.1021/jm401053m.

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23

Funk, Michael A. "Itaconate brings metalloenzyme to a halt." Science 366, no. 6465 (October 31, 2019): 583.13–585. http://dx.doi.org/10.1126/science.366.6465.583-m.

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24

Armstrong, Richard N. "Mechanistic Diversity in a Metalloenzyme Superfamily†." Biochemistry 39, no. 45 (November 2000): 13625–32. http://dx.doi.org/10.1021/bi001814v.

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25

Koder, Ronald L., Bernard Everson, Lei Zhang, Jonathan Preston, and Emma Bjerkefeldt. "Optimizing Protein Dynamics in Metalloenzyme Design." Biophysical Journal 112, no. 3 (February 2017): 193a. http://dx.doi.org/10.1016/j.bpj.2016.11.1072.

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26

Haeggström, Jesper Z., Anders Wetterholm, Robert Shapiro, Bert L. Vallee, and Bengt Samuelsson. "Leukotriene A4 hydrolase: A zinc metalloenzyme." Biochemical and Biophysical Research Communications 172, no. 3 (November 1990): 965–70. http://dx.doi.org/10.1016/0006-291x(90)91540-9.

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27

Grubmeyer, Charles, Marios Skiadopoulos, and Alan E. Senior. "l-Histidinol dehydrogenase, a Zn2+-metalloenzyme." Archives of Biochemistry and Biophysics 272, no. 2 (August 1989): 311–17. http://dx.doi.org/10.1016/0003-9861(89)90224-5.

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28

Okamoto, Yasunori, and Thomas R. Ward. "Cross-Regulation of an Artificial Metalloenzyme." Angewandte Chemie 129, no. 34 (May 31, 2017): 10290–94. http://dx.doi.org/10.1002/ange.201702181.

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29

Dong, Steven D., and Ronald Breslow. "ChemInform Abstract: Bifunctional Cyclodextrin Metalloenzyme Mimics." ChemInform 30, no. 10 (June 17, 2010): no. http://dx.doi.org/10.1002/chin.199910229.

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30

Okamoto, Yasunori, and Thomas R. Ward. "Cross-Regulation of an Artificial Metalloenzyme." Angewandte Chemie International Edition 56, no. 34 (May 31, 2017): 10156–60. http://dx.doi.org/10.1002/anie.201702181.

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31

Karges, Johannes, Ryjul W. Stokes, and Seth M. Cohen. "Photorelease of a metal-binding pharmacophore from a Ru(ii) polypyridine complex." Dalton Transactions 50, no. 8 (2021): 2757–65. http://dx.doi.org/10.1039/d0dt04290k.

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32

Zhang, Yaoyao, Weiying Wang, Wenqin Fu, Mingjie Zhang, Zhiyang Tang, Rong Tan, and Donghong Yin. "Titanium(iv)-folded single-chain polymeric nanoparticles as artificial metalloenzyme for asymmetric sulfoxidation in water." Chemical Communications 54, no. 68 (2018): 9430–33. http://dx.doi.org/10.1039/c8cc05590d.

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33

Schneider, Camille R., Anastasia C. Manesis, Michael J. Stevenson, and Hannah S. Shafaat. "A photoactive semisynthetic metalloenzyme exhibits complete selectivity for CO2 reduction in water." Chemical Communications 54, no. 37 (2018): 4681–84. http://dx.doi.org/10.1039/c8cc01297k.

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34

Horch, Marius, Ana Filipa Pinto, Maria Andrea Mroginski, Miguel Teixeira, Peter Hildebrandt, and Ingo Zebger. "Metal-induced histidine deprotonation in biocatalysis? Experimental and theoretical insights into superoxide reductase." RSC Adv. 4, no. 96 (2014): 54091–95. http://dx.doi.org/10.1039/c4ra11976b.

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35

Cheng, Wenting, Jiehua Ma, Yongchen Zhang, Chuanjun Xu, Zhaoli Zhang, Liang Hu, and Jinlong Li. "Bio-inspired construction of a semi-artificial enzyme complex for detecting histone acetyltransferases activity." Analyst 145, no. 2 (2020): 613–18. http://dx.doi.org/10.1039/c9an01896d.

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36

Mus, Florence, Alexander B. Alleman, Natasha Pence, Lance C. Seefeldt, and John W. Peters. "Exploring the alternatives of biological nitrogen fixation." Metallomics 10, no. 4 (2018): 523–38. http://dx.doi.org/10.1039/c8mt00038g.

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37

Li, Yinghao, Changhao Wang, Jingya Hao, Mingpan Cheng, Guoqing Jia, and Can Li. "Higher-order human telomeric G-quadruplex DNA metalloenzyme catalyzed Diels–Alder reaction: an unexpected inversion of enantioselectivity modulated by K+ and NH4+ ions." Chemical Communications 51, no. 67 (2015): 13174–77. http://dx.doi.org/10.1039/c5cc05215g.

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38

Dick, Benjamin L., Ashay Patel, and Seth M. Cohen. "Effect of heterocycle content on metal binding isostere coordination." Chemical Science 11, no. 26 (2020): 6907–14. http://dx.doi.org/10.1039/d0sc02717k.

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39

Harty, Matthew L., Amar Nath Sharma, and Stephen L. Bearne. "Catalytic properties of the metal ion variants of mandelate racemase reveal alterations in the apparent electrophilicity of the metal cofactor." Metallomics 11, no. 3 (2019): 707–23. http://dx.doi.org/10.1039/c8mt00330k.

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40

Albareda, Marta, Agnès Rodrigue, Belén Brito, Tomás Ruiz-Argüeso, Juan Imperial, Marie-Andrée Mandrand-Berthelot, and Jose Palacios. "Rhizobium leguminosarum HupE is a highly-specific diffusion facilitator for nickel uptake." Metallomics 7, no. 4 (2015): 691–701. http://dx.doi.org/10.1039/c4mt00298a.

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Functional and topological analysis ofRhizobium leguminosarumHupE, the founding member of the HupE/UreJ family of nickel permeases, provides new hints on how bacteria manage nickel provision for metalloenzyme synthesis.

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41

Zambrano, Gerardo, Alina Sekretareva, Daniele D'Alonzo, Linda Leone, Vincenzo Pavone, Angela Lombardi, and Flavia Nastri. "Oxidative dehalogenation of trichlorophenol catalyzed by a promiscuous artificial heme-enzyme." RSC Advances 12, no. 21 (2022): 12947–56. http://dx.doi.org/10.1039/d2ra00811d.

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The artificial metalloenzyme FeMC6*a is able to perform the H2O2-mediated dechlorination of 2,4,6-trichlorophenol with unrivalled catalytic efficiency, highlighting its potential application for the removal of toxic pollutants.

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42

Herrero, Christian, Annamaria Quaranta, Rémy Ricoux, Alexandre Trehoux, Atif Mahammed, Zeev Gross, Frédéric Banse, and Jean-Pierre Mahy. "Oxidation catalysis via visible-light water activation of a [Ru(bpy)3]2+ chromophore BSA–metallocorrole couple." Dalton Transactions 45, no. 2 (2016): 706–10. http://dx.doi.org/10.1039/c5dt04158a.

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Light induced enantioselective oxidation of thioanisole with water as the oxygen atom source is catalyzed by a Mn-corrole–BSA artificial metalloenzyme in the presence of a photoactivable ruthenium complex.

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43

Laureanti, Joseph A., Qiwen Su, and Wendy J. Shaw. "A protein scaffold enables hydrogen evolution for a Ni-bisdiphosphine complex." Dalton Transactions 50, no. 43 (2021): 15754–59. http://dx.doi.org/10.1039/d1dt03295j.

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An artificial metalloenzyme acting as a functional biomimic of hydrogenase enzymes was activated by assembly via covalent attachment of the molecular complex, [Ni(PNglycineP)2]2−, within a structured protein scaffold.

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44

Honarmand Ebrahimi, Kourosh. "A unifying view of the broad-spectrum antiviral activity of RSAD2 (viperin) based on its radical-SAM chemistry." Metallomics 10, no. 4 (2018): 539–52. http://dx.doi.org/10.1039/c7mt00341b.

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45

Kim, Sung-Kun, Cynthe L. Sims, Susan E. Wozniak, Stephanie H. Drude, Dustin Whitson, and Robert W. Shaw. "Antibiotic Resistance in Bacteria: Novel Metalloenzyme Inhibitors." Chemical Biology & Drug Design 74, no. 4 (October 2009): 343–48. http://dx.doi.org/10.1111/j.1747-0285.2009.00879.x.

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46

Pordea, Anca. "Metal-binding promiscuity in artificial metalloenzyme design." Current Opinion in Chemical Biology 25 (April 2015): 124–32. http://dx.doi.org/10.1016/j.cbpa.2014.12.035.

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47

Cuenoud, Bernard, and Jack W. Szostak. "A DNA metalloenzyme with DNA ligase activity." Nature 375, no. 6532 (June 1995): 611–14. http://dx.doi.org/10.1038/375611a0.

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48

Colpas, G. J., M. Kumar, and M. J. Maroney. "XAS structural investigations of NI metalloenzyme models." Journal of Inorganic Biochemistry 36, no. 3-4 (August 1989): 249. http://dx.doi.org/10.1016/0162-0134(89)84303-x.

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49

Whittaker, James W. "Molecular relaxation and metalloenzyme active site modeling." International Journal of Quantum Chemistry 90, no. 4-5 (2002): 1529–35. http://dx.doi.org/10.1002/qua.10422.

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50

Heinisch, Tillmann, and Thomas R. Ward. "Latest Developments in Metalloenzyme Design and Repurposing." European Journal of Inorganic Chemistry 2015, no. 21 (June 18, 2015): 3406–18. http://dx.doi.org/10.1002/ejic.201500408.

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