Artigos de revistas sobre o 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.º 16 (18 de junho de 2010): 4143–52. http://dx.doi.org/10.1128/jb.00270-10.
Texto completo da fonteBoll, 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.º 10 (1 de outubro de 2005): 999–1006. http://dx.doi.org/10.1515/bc.2005.116.
Texto completo da fonteSeelmann, Carola S., Max Willistein, Johann Heider e Matthias Boll. "Tungstoenzymes: Occurrence, Catalytic Diversity and Cofactor Synthesis". Inorganics 8, n.º 8 (31 de julho de 2020): 44. http://dx.doi.org/10.3390/inorganics8080044.
Texto completo da fonteDavies, 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.º 21 (1998): 3647–56. http://dx.doi.org/10.1039/a805688i.
Texto completo da fontePushie, M. Jake, e Graham N. George. "Spectroscopic studies of molybdenum and tungsten enzymes". Coordination Chemistry Reviews 255, n.º 9-10 (maio de 2011): 1055–84. http://dx.doi.org/10.1016/j.ccr.2011.01.056.
Texto completo da fonteGeorge, 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.º 2-3 (agosto de 1991): 241. http://dx.doi.org/10.1016/0162-0134(91)84231-w.
Texto completo da fonteScott, 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.º 20 (14 de agosto de 2015): 7339–47. http://dx.doi.org/10.1128/aem.01634-15.
Texto completo da fonteYang, Jing, John H. Enemark e Martin L. Kirk. "Metal–Dithiolene Bonding Contributions to Pyranopterin Molybdenum Enzyme Reactivity". Inorganics 8, n.º 3 (5 de março de 2020): 19. http://dx.doi.org/10.3390/inorganics8030019.
Texto completo da fonteLeimkühler, Silke. "Metal-Containing Formate Dehydrogenases, a Personal View". Molecules 28, n.º 14 (11 de julho de 2023): 5338. http://dx.doi.org/10.3390/molecules28145338.
Texto completo da fonteBrondino, 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.º 2 (abril de 2006): 109–14. http://dx.doi.org/10.1016/j.cbpa.2006.01.034.
Texto completo da fonteHagen, Wilfred R. "The Development of Tungsten Biochemistry—A Personal Recollection". Molecules 28, n.º 10 (11 de maio de 2023): 4017. http://dx.doi.org/10.3390/molecules28104017.
Texto completo da fonteSchulzke, Carola, e Christian Fischer. "Molybdenum and tungsten oxidoreductase model chemistry". Acta Crystallographica Section A Foundations and Advances 70, a1 (5 de agosto de 2014): C1372. http://dx.doi.org/10.1107/s2053273314086276.
Texto completo da fonteSohail, 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.º 1 (26 de março de 2020): 1–45. http://dx.doi.org/10.1515/revic-2019-0013.
Texto completo da fonteAkbassova, 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.º 3 (16 de outubro de 2023): 48–59. http://dx.doi.org/10.11134/btp.3.2023.6.
Texto completo da fonteMukhamejanova, 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 de julho de 2021): 632–38. http://dx.doi.org/10.5219/1665.
Texto completo da fonteRomão, Maria João. "Molybdenum and tungsten enzymes: a crystallographic and mechanistic overview". Dalton Transactions, n.º 21 (2009): 4053. http://dx.doi.org/10.1039/b821108f.
Texto completo da fonteMcMaster, J., e John H. Enemark. "The active sites of molybdenum- and tungsten-containing enzymes". Current Opinion in Chemical Biology 2, n.º 2 (abril de 1998): 201–7. http://dx.doi.org/10.1016/s1367-5931(98)80061-6.
Texto completo da fonteCordas, Cristina M., e José J. G. Moura. "Molybdenum and tungsten enzymes redox properties – A brief overview". Coordination Chemistry Reviews 394 (setembro de 2019): 53–64. http://dx.doi.org/10.1016/j.ccr.2019.05.005.
Texto completo da fonteBoll, 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.º 1-3 (2016): 119–37. http://dx.doi.org/10.1159/000440805.
Texto completo da fonteRoy, 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.º 4 (15 de fevereiro de 1999): 1171–80. http://dx.doi.org/10.1128/jb.181.4.1171-1180.1999.
Texto completo da fonteYergaliev, T. "Molybdenum and plant resistance to viral infection". BULLETIN of the L.N. Gumilyov Eurasian National University. BIOSCIENCE Series 135, n.º 2 (2021): 63–70. http://dx.doi.org/10.32523/2616-7034-2021-135-2-63-70.
Texto completo da fonteMoura, 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.º 2 (11 de fevereiro de 2015): 181–82. http://dx.doi.org/10.1007/s00775-015-1243-9.
Texto completo da fonteRothery, 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.º 37 (27 de agosto de 2012): 14773–78. http://dx.doi.org/10.1073/pnas.1200671109.
Texto completo da fonteRoy, Roopali, e Michael W. W. Adams. "Characterization of a Fourth Tungsten-Containing Enzyme from the Hyperthermophilic Archaeon Pyrococcus furiosus". Journal of Bacteriology 184, n.º 24 (15 de dezembro de 2002): 6952–56. http://dx.doi.org/10.1128/jb.184.24.6952-6956.2002.
Texto completo da fonteGrant, 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 de maio de 2021): 517–30. http://dx.doi.org/10.22203/ecm.v041a33.
Texto completo da fonteBurgmayer, Sharon J. Nieter, e Martin L. Kirk. "Advancing Our Understanding of Pyranopterin-Dithiolene Contributions to Moco Enzyme Catalysis". Molecules 28, n.º 22 (7 de novembro de 2023): 7456. http://dx.doi.org/10.3390/molecules28227456.
Texto completo da fonteYoung, Charles G., e Anthony G. Wedd. "Metal chemistry relevant to the mononuclear molybdenum and tungsten pterin enzymes". Chemical Communications, n.º 14 (1997): 1251–57. http://dx.doi.org/10.1039/a606660g.
Texto completo da fonteENEMARK, J. H., e C. G. YOUNG. "ChemInform Abstract: Bioinorganic Chemistry of Pterin-Containing Molybdenum and Tungsten Enzymes." ChemInform 25, n.º 43 (18 de agosto de 2010): no. http://dx.doi.org/10.1002/chin.199443309.
Texto completo da fonteSihombing, 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.º 3 (26 de maio de 2021): 325. http://dx.doi.org/10.29303/jppipa.v7i3.699.
Texto completo da fonteSugimoto, 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.º 1 (janeiro de 2008): 77–80. http://dx.doi.org/10.1016/j.inoche.2007.10.020.
Texto completo da fonteS, 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 de dezembro de 2021): 370–76. http://dx.doi.org/10.29303/jppipa.v7ispecialissue.1248.
Texto completo da fonteFogeron, Thibault, Yun Li e Marc Fontecave. "Formate Dehydrogenase Mimics as Catalysts for Carbon Dioxide Reduction". Molecules 27, n.º 18 (14 de setembro de 2022): 5989. http://dx.doi.org/10.3390/molecules27185989.
Texto completo da fonteSosorova, 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.º 7 (20 de julho de 2021): 48–53. http://dx.doi.org/10.18412/1816-0395-2021-7-48-53.
Texto completo da fonteStiefel, E. I. "Transition metal sulfur chemistry and its relvance to molybdenum and tungsten enzymes". Journal of Inorganic Biochemistry 67, n.º 1-4 (julho de 1997): 8. http://dx.doi.org/10.1016/s0162-0134(97)89891-1.
Texto completo da fonteMajumdar, Amit, e Sabyasachi Sarkar. "Bioinorganic chemistry of molybdenum and tungsten enzymes: A structural–functional modeling approach". Coordination Chemistry Reviews 255, n.º 9-10 (maio de 2011): 1039–54. http://dx.doi.org/10.1016/j.ccr.2010.11.027.
Texto completo da fonteStiefel, E. I. "Transition metal sulfur chemistry and its relevance to molybdenum and tungsten enzymes". Pure and Applied Chemistry 70, n.º 4 (1 de janeiro de 1998): 889–96. http://dx.doi.org/10.1351/pac199870040889.
Texto completo da fonteSerikovna, 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.º 1 (23 de janeiro de 2024): 261–70. http://dx.doi.org/10.53894/ijirss.v7i1.2616.
Texto completo da fontePark, Myong-Ok, Taeko Mizutani e Patrik R. Jones. "Glyceraldehyde-3-Phosphate Ferredoxin Oxidoreductase from Methanococcus maripaludis". Journal of Bacteriology 189, n.º 20 (17 de agosto de 2007): 7281–89. http://dx.doi.org/10.1128/jb.00828-07.
Texto completo da fonteJoshi, 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.º 7 (24 de março de 2003): 3719–24. http://dx.doi.org/10.1073/pnas.0636832100.
Texto completo da fonteYOUNG, C. G., e A. G. WEDD. "ChemInform Abstract: Metal Chemistry Relevant to the Mononuclear Molybdenum and Tungsten Pterin Enzymes". ChemInform 28, n.º 42 (3 de agosto de 2010): no. http://dx.doi.org/10.1002/chin.199742321.
Texto completo da fonteTokasheva, 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.º 4 (2021): 84–91. http://dx.doi.org/10.32523/2616-7034-2021-137-4-84-91.
Texto completo da fonteSugimoto, 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.º 21 (outubro de 2007): 8460–62. http://dx.doi.org/10.1021/ic7012733.
Texto completo da fonteHuwiler, 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.º 6 (23 de janeiro de 2019): 2259–64. http://dx.doi.org/10.1073/pnas.1819636116.
Texto completo da fonteBurgmayer, Sharon. "Making Moco: A Personal History". Molecules 28, n.º 21 (27 de outubro de 2023): 7296. http://dx.doi.org/10.3390/molecules28217296.
Texto completo da fonteMaia, Luisa B. "Bringing Nitric Oxide to the Molybdenum World—A Personal Perspective". Molecules 28, n.º 15 (2 de agosto de 2023): 5819. http://dx.doi.org/10.3390/molecules28155819.
Texto completo da fonteHolm, 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.º 9-10 (maio de 2011): 993–1015. http://dx.doi.org/10.1016/j.ccr.2010.10.017.
Texto completo da fonteSugimoto, 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.
Texto completo da fontePermyakov, Eugene A. "Metal Binding Proteins". Encyclopedia 1, n.º 1 (15 de março de 2021): 261–92. http://dx.doi.org/10.3390/encyclopedia1010024.
Texto completo da fonteHochheimer, 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.º 3 (dezembro de 1995): 910–20. http://dx.doi.org/10.1111/j.1432-1033.1995.910_a.x.
Texto completo da fonteSugimoto, 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.º 9 (2013): 3059–70. http://dx.doi.org/10.1039/c2dt32179c.
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