Articoli di riviste sul tema "Tungsten enzymes"
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Sevcenco, Ana-Maria, Loes E. Bevers, Martijn W. H. Pinkse, Gerard C. Krijger, Hubert T. Wolterbeek, Peter D. E. M. Verhaert, Wilfred R. Hagen e Peter-Leon Hagedoorn. "Molybdenum Incorporation in Tungsten Aldehyde Oxidoreductase Enzymes from Pyrococcus furiosus". Journal of Bacteriology 192, n. 16 (18 giugno 2010): 4143–52. http://dx.doi.org/10.1128/jb.00270-10.
Testo completoBoll, Matthias, Bernhard Schink, Albrecht Messerschmidt e Peter M. H. Kroneck. "Novel bacterial molybdenum and tungsten enzymes: three-dimensional structure, spectroscopy, and reaction mechanism". Biological Chemistry 386, n. 10 (1 ottobre 2005): 999–1006. http://dx.doi.org/10.1515/bc.2005.116.
Testo completoSeelmann, Carola S., Max Willistein, Johann Heider e Matthias Boll. "Tungstoenzymes: Occurrence, Catalytic Diversity and Cofactor Synthesis". Inorganics 8, n. 8 (31 luglio 2020): 44. http://dx.doi.org/10.3390/inorganics8080044.
Testo completoDavies, E. Stephen, Georgina M. Aston, Roy L. Beddoes, David Collison, Andrew Dinsmore, Arefa Docrat, John A. Joule, Clare R. Wilson e C. David Garner. "Oxo–tungsten bis-dithiolene complexes relevant to tungsten centres in enzymes". Journal of the Chemical Society, Dalton Transactions, n. 21 (1998): 3647–56. http://dx.doi.org/10.1039/a805688i.
Testo completoPushie, M. Jake, e Graham N. George. "Spectroscopic studies of molybdenum and tungsten enzymes". Coordination Chemistry Reviews 255, n. 9-10 (maggio 2011): 1055–84. http://dx.doi.org/10.1016/j.ccr.2011.01.056.
Testo completoGeorge, G. N., Y. Gea, R. C. Prince, S. Mukund e M. W. W. Adams. "Tungsten oxo-thiolate enzymes from hyperthermophilic bacteria." Journal of Inorganic Biochemistry 43, n. 2-3 (agosto 1991): 241. http://dx.doi.org/10.1016/0162-0134(91)84231-w.
Testo completoScott, Israel M., Gabe M. Rubinstein, Gina L. Lipscomb, Mirko Basen, Gerrit J. Schut, Amanda M. Rhaesa, W. Andrew Lancaster, Farris L. Poole, Robert M. Kelly e Michael W. W. Adams. "A New Class of Tungsten-Containing Oxidoreductase in Caldicellulosiruptor, a Genus of Plant Biomass-Degrading Thermophilic Bacteria". Applied and Environmental Microbiology 81, n. 20 (14 agosto 2015): 7339–47. http://dx.doi.org/10.1128/aem.01634-15.
Testo completoYang, Jing, John H. Enemark e Martin L. Kirk. "Metal–Dithiolene Bonding Contributions to Pyranopterin Molybdenum Enzyme Reactivity". Inorganics 8, n. 3 (5 marzo 2020): 19. http://dx.doi.org/10.3390/inorganics8030019.
Testo completoLeimkühler, Silke. "Metal-Containing Formate Dehydrogenases, a Personal View". Molecules 28, n. 14 (11 luglio 2023): 5338. http://dx.doi.org/10.3390/molecules28145338.
Testo completoBrondino, Carlos D., Maria João Romão, Isabel Moura e José JG Moura. "Molybdenum and tungsten enzymes: the xanthine oxidase family". Current Opinion in Chemical Biology 10, n. 2 (aprile 2006): 109–14. http://dx.doi.org/10.1016/j.cbpa.2006.01.034.
Testo completoHagen, Wilfred R. "The Development of Tungsten Biochemistry—A Personal Recollection". Molecules 28, n. 10 (11 maggio 2023): 4017. http://dx.doi.org/10.3390/molecules28104017.
Testo completoSchulzke, Carola, e Christian Fischer. "Molybdenum and tungsten oxidoreductase model chemistry". Acta Crystallographica Section A Foundations and Advances 70, a1 (5 agosto 2014): C1372. http://dx.doi.org/10.1107/s2053273314086276.
Testo completoSohail, Muhammad, Muhammad Zeshan Ashraf, Raziya Nadeem, Shamsa Bibi, Rabia Rehman e Muhammad Adnan Iqbal. "Techniques in the synthesis of organometallic compounds of tungsten". Reviews in Inorganic Chemistry 40, n. 1 (26 marzo 2020): 1–45. http://dx.doi.org/10.1515/revic-2019-0013.
Testo completoAkbassova, A., M. Beisekova, A. Tassanbiyeva, D. Zhamshitova, A. Kurmanbayeva, S. Zhangazin, N. Moldakimova, A. Shalabayeva, Zh Masalimov e A. Akbassova. "COMBINED EFFECT OF TBSV P19 MUTANTS AND HEAVY METALS ON ANTIOXIDANT ENZYME ACTIVITY". Eurasian Journal of Applied Biotechnology, n. 3 (16 ottobre 2023): 48–59. http://dx.doi.org/10.11134/btp.3.2023.6.
Testo completoMukhamejanova, Akmaral, Zerekbay Alikulov, Bakyt Tuganova e Zhanna Adamzhanova. "The xanthine oxidase and its associated activities in the ovine milk and liver: distinctive in impact of in vivo molybdenum". Potravinarstvo Slovak Journal of Food Sciences 15 (12 luglio 2021): 632–38. http://dx.doi.org/10.5219/1665.
Testo completoRomão, Maria João. "Molybdenum and tungsten enzymes: a crystallographic and mechanistic overview". Dalton Transactions, n. 21 (2009): 4053. http://dx.doi.org/10.1039/b821108f.
Testo completoMcMaster, J., e John H. Enemark. "The active sites of molybdenum- and tungsten-containing enzymes". Current Opinion in Chemical Biology 2, n. 2 (aprile 1998): 201–7. http://dx.doi.org/10.1016/s1367-5931(98)80061-6.
Testo completoCordas, Cristina M., e José J. G. Moura. "Molybdenum and tungsten enzymes redox properties – A brief overview". Coordination Chemistry Reviews 394 (settembre 2019): 53–64. http://dx.doi.org/10.1016/j.ccr.2019.05.005.
Testo completoBoll, Matthias, Oliver Einsle, Ulrich Ermler, Peter M. H. Kroneck e G. Matthias Ullmann. "Structure and Function of the Unusual Tungsten Enzymes Acetylene Hydratase and Class II Benzoyl-Coenzyme A Reductase". Journal of Molecular Microbiology and Biotechnology 26, n. 1-3 (2016): 119–37. http://dx.doi.org/10.1159/000440805.
Testo completoRoy, Roopali, Swarnalatha Mukund, Gerrit J. Schut, Dianne M. Dunn, Robert Weiss e Michael W. W. Adams. "Purification and Molecular Characterization of the Tungsten-Containing Formaldehyde Ferredoxin Oxidoreductase from the Hyperthermophilic Archaeon Pyrococcus furiosus: the Third of a Putative Five-Member Tungstoenzyme Family". Journal of Bacteriology 181, n. 4 (15 febbraio 1999): 1171–80. http://dx.doi.org/10.1128/jb.181.4.1171-1180.1999.
Testo completoYergaliev, T. "Molybdenum and plant resistance to viral infection". BULLETIN of the L.N. Gumilyov Eurasian National University. BIOSCIENCE Series 135, n. 2 (2021): 63–70. http://dx.doi.org/10.32523/2616-7034-2021-135-2-63-70.
Testo completoMoura, José J. G., Paul V. Bernhardt, Luísa B. Maia e Pablo J. Gonzalez. "Molybdenum and tungsten enzymes: from biology to chemistry and back". JBIC Journal of Biological Inorganic Chemistry 20, n. 2 (11 febbraio 2015): 181–82. http://dx.doi.org/10.1007/s00775-015-1243-9.
Testo completoRothery, R. A., B. Stein, M. Solomonson, M. L. Kirk e J. H. Weiner. "Pyranopterin conformation defines the function of molybdenum and tungsten enzymes". Proceedings of the National Academy of Sciences 109, n. 37 (27 agosto 2012): 14773–78. http://dx.doi.org/10.1073/pnas.1200671109.
Testo completoRoy, Roopali, e Michael W. W. Adams. "Characterization of a Fourth Tungsten-Containing Enzyme from the Hyperthermophilic Archaeon Pyrococcus furiosus". Journal of Bacteriology 184, n. 24 (15 dicembre 2002): 6952–56. http://dx.doi.org/10.1128/jb.184.24.6952-6956.2002.
Testo completoGrant, MP, CR VanderSchee, H. Chou, A. Bolt, LM Epure, D. Kuter, J. Antoniou, S. Bohle, KK Mann e F. Mwale. "Tungsten accumulates in the intervertebral disc and vertebrae stimulating disc degeneration and upregulating markers of inflammation and pain". European Cells and Materials 41 (17 maggio 2021): 517–30. http://dx.doi.org/10.22203/ecm.v041a33.
Testo completoBurgmayer, Sharon J. Nieter, e Martin L. Kirk. "Advancing Our Understanding of Pyranopterin-Dithiolene Contributions to Moco Enzyme Catalysis". Molecules 28, n. 22 (7 novembre 2023): 7456. http://dx.doi.org/10.3390/molecules28227456.
Testo completoYoung, Charles G., e Anthony G. Wedd. "Metal chemistry relevant to the mononuclear molybdenum and tungsten pterin enzymes". Chemical Communications, n. 14 (1997): 1251–57. http://dx.doi.org/10.1039/a606660g.
Testo completoENEMARK, J. H., e C. G. YOUNG. "ChemInform Abstract: Bioinorganic Chemistry of Pterin-Containing Molybdenum and Tungsten Enzymes." ChemInform 25, n. 43 (18 agosto 2010): no. http://dx.doi.org/10.1002/chin.199443309.
Testo completoSihombing, Victor H., e Abd Hakim S. "The Use of Tungsten in Potentiometry to Detect Pospat Baffer and Urease Enzyme". Jurnal Penelitian Pendidikan IPA 7, n. 3 (26 maggio 2021): 325. http://dx.doi.org/10.29303/jppipa.v7i3.699.
Testo completoSugimoto, Hideki, e Kunihisa Sugimoto. "New bis(pyranodithiolene) tungsten(IV) and (VI) complexes as chemical analogues of the active sites of tungsten enzymes". Inorganic Chemistry Communications 11, n. 1 (gennaio 2008): 77–80. http://dx.doi.org/10.1016/j.inoche.2007.10.020.
Testo completoS, Abd Hakim. "Characterization of PVA-Enzyme Coated Indicator Electrodes GA coated again with PVC-KTpClPB-o-NPOE UV-Vis analysis, variable signal analysis, sensor sensitivity and SEM-EDS". Jurnal Penelitian Pendidikan IPA 7, SpecialIssue (26 dicembre 2021): 370–76. http://dx.doi.org/10.29303/jppipa.v7ispecialissue.1248.
Testo completoFogeron, Thibault, Yun Li e Marc Fontecave. "Formate Dehydrogenase Mimics as Catalysts for Carbon Dioxide Reduction". Molecules 27, n. 18 (14 settembre 2022): 5989. http://dx.doi.org/10.3390/molecules27185989.
Testo completoSosorova, S. B., I. N. Lavrent’eva, L. N. Boloneva, V. L. Ubugunov e E. G. Tsyrempilov. "Enzymative Activity of Soils in the Activity Territory of the Dzhida Tungsten-Molybdenum Combine (Western Zabaikalie)". Ecology and Industry of Russia 25, n. 7 (20 luglio 2021): 48–53. http://dx.doi.org/10.18412/1816-0395-2021-7-48-53.
Testo completoStiefel, E. I. "Transition metal sulfur chemistry and its relvance to molybdenum and tungsten enzymes". Journal of Inorganic Biochemistry 67, n. 1-4 (luglio 1997): 8. http://dx.doi.org/10.1016/s0162-0134(97)89891-1.
Testo completoMajumdar, Amit, e Sabyasachi Sarkar. "Bioinorganic chemistry of molybdenum and tungsten enzymes: A structural–functional modeling approach". Coordination Chemistry Reviews 255, n. 9-10 (maggio 2011): 1039–54. http://dx.doi.org/10.1016/j.ccr.2010.11.027.
Testo completoStiefel, E. I. "Transition metal sulfur chemistry and its relevance to molybdenum and tungsten enzymes". Pure and Applied Chemistry 70, n. 4 (1 gennaio 1998): 889–96. http://dx.doi.org/10.1351/pac199870040889.
Testo completoSerikovna, Tokasheva Dana, Akbassova Alya Zholdasbayevna e Omarov Rustem Tukenovich. "Molybdenum and tungsten stimulate immune responses under biotic stress in Nicotiana abenthamiana infected with tomato bushy stunt virus". International Journal of Innovative Research and Scientific Studies 7, n. 1 (23 gennaio 2024): 261–70. http://dx.doi.org/10.53894/ijirss.v7i1.2616.
Testo completoPark, Myong-Ok, Taeko Mizutani e Patrik R. Jones. "Glyceraldehyde-3-Phosphate Ferredoxin Oxidoreductase from Methanococcus maripaludis". Journal of Bacteriology 189, n. 20 (17 agosto 2007): 7281–89. http://dx.doi.org/10.1128/jb.00828-07.
Testo completoJoshi, H. K., J. J. A. Cooney, F. E. Inscore, N. E. Gruhn, D. L. Lichtenberger e J. H. Enemark. "Investigation of metal-dithiolate fold angle effects: Implications for molybdenum and tungsten enzymes". Proceedings of the National Academy of Sciences 100, n. 7 (24 marzo 2003): 3719–24. http://dx.doi.org/10.1073/pnas.0636832100.
Testo completoYOUNG, C. G., e A. G. WEDD. "ChemInform Abstract: Metal Chemistry Relevant to the Mononuclear Molybdenum and Tungsten Pterin Enzymes". ChemInform 28, n. 42 (3 agosto 2010): no. http://dx.doi.org/10.1002/chin.199742321.
Testo completoTokasheva, D. S., M. K. Beisekova, K. E. Zhanassova, Zh B. Tleukulova, A. Zh Akbasova e R. T. Omarov. "Influence of various molybdenum, tungsten, and molybdenum with tungsten concentrations to the growth of Nicotiana Benthamiana". BULLETIN of the L.N. Gumilyov Eurasian National University. BIOSCIENCE Series 137, n. 4 (2021): 84–91. http://dx.doi.org/10.32523/2616-7034-2021-137-4-84-91.
Testo completoSugimoto, Hideki, Hiroyuki Tano, Reiko Tajima, Hiroyuki Miyake, Hiroshi Tsukube, Hiromi Ohi e Shinobu Itoh. "In Situ Generation of Oxo−sulfidobis(dithiolene)tungsten(VI) Complexes: Active-Site Models for the Aldehyde Ferredoxin Oxidoreductase Family of Tungsten Enzymes". Inorganic Chemistry 46, n. 21 (ottobre 2007): 8460–62. http://dx.doi.org/10.1021/ic7012733.
Testo completoHuwiler, Simona G., Claudia Löffler, Sebastian E. L. Anselmann, Hans-Joachim Stärk, Martin von Bergen, Jennifer Flechsler, Reinhard Rachel e Matthias Boll. "One-megadalton metalloenzyme complex inGeobacter metallireducensinvolved in benzene ring reduction beyond the biological redox window". Proceedings of the National Academy of Sciences 116, n. 6 (23 gennaio 2019): 2259–64. http://dx.doi.org/10.1073/pnas.1819636116.
Testo completoBurgmayer, Sharon. "Making Moco: A Personal History". Molecules 28, n. 21 (27 ottobre 2023): 7296. http://dx.doi.org/10.3390/molecules28217296.
Testo completoMaia, Luisa B. "Bringing Nitric Oxide to the Molybdenum World—A Personal Perspective". Molecules 28, n. 15 (2 agosto 2023): 5819. http://dx.doi.org/10.3390/molecules28155819.
Testo completoHolm, Richard H., Edward I. Solomon, Amit Majumdar e Adam Tenderholt. "Comparative molecular chemistry of molybdenum and tungsten and its relation to hydroxylase and oxotransferase enzymes". Coordination Chemistry Reviews 255, n. 9-10 (maggio 2011): 993–1015. http://dx.doi.org/10.1016/j.ccr.2010.10.017.
Testo completoSugimoto, Hideki. "Chemistry of Synthetic Models Relevant to the Active Sites of Molybdenum and Tungsten Containing Enzymes". Bulletin of Japan Society of Coordination Chemistry 50 (2007): 26–39. http://dx.doi.org/10.4019/bjscc.50.26.
Testo completoPermyakov, Eugene A. "Metal Binding Proteins". Encyclopedia 1, n. 1 (15 marzo 2021): 261–92. http://dx.doi.org/10.3390/encyclopedia1010024.
Testo completoHochheimer, Andreas, Ruth A. Schmitz, Rudolf K. Thauer e Reiner Hedderich. "The Tungsten Formylmethanofuran Dehydrogenase from Methanobacterium Thermoautotrophicum Contains Sequence Motifs Characteristic for Enzymes Containing Molybdopterin Dinucleotide". European Journal of Biochemistry 234, n. 3 (dicembre 1995): 910–20. http://dx.doi.org/10.1111/j.1432-1033.1995.910_a.x.
Testo completoSugimoto, Hideki, Kohei Hatakeda, Kazuo Toyota, Susumu Tatemoto, Minoru Kubo, Takashi Ogura e Shinobu Itoh. "A new series of bis(ene-1,2-dithiolato)tungsten(iv), -(v), -(vi) complexes as reaction centre models of tungsten enzymes: Preparation, crystal structures and spectroscopic properties". Dalton Trans. 42, n. 9 (2013): 3059–70. http://dx.doi.org/10.1039/c2dt32179c.
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