Journal articles on the topic '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, and Peter-Leon Hagedoorn. "Molybdenum Incorporation in Tungsten Aldehyde Oxidoreductase Enzymes from Pyrococcus furiosus." Journal of Bacteriology 192, no. 16 (June 18, 2010): 4143–52. http://dx.doi.org/10.1128/jb.00270-10.
Full textBoll, Matthias, Bernhard Schink, Albrecht Messerschmidt, and Peter M. H. Kroneck. "Novel bacterial molybdenum and tungsten enzymes: three-dimensional structure, spectroscopy, and reaction mechanism." Biological Chemistry 386, no. 10 (October 1, 2005): 999–1006. http://dx.doi.org/10.1515/bc.2005.116.
Full textSeelmann, Carola S., Max Willistein, Johann Heider, and Matthias Boll. "Tungstoenzymes: Occurrence, Catalytic Diversity and Cofactor Synthesis." Inorganics 8, no. 8 (July 31, 2020): 44. http://dx.doi.org/10.3390/inorganics8080044.
Full textDavies, E. Stephen, Georgina M. Aston, Roy L. Beddoes, David Collison, Andrew Dinsmore, Arefa Docrat, John A. Joule, Clare R. Wilson, and C. David Garner. "Oxo–tungsten bis-dithiolene complexes relevant to tungsten centres in enzymes." Journal of the Chemical Society, Dalton Transactions, no. 21 (1998): 3647–56. http://dx.doi.org/10.1039/a805688i.
Full textPushie, M. Jake, and Graham N. George. "Spectroscopic studies of molybdenum and tungsten enzymes." Coordination Chemistry Reviews 255, no. 9-10 (May 2011): 1055–84. http://dx.doi.org/10.1016/j.ccr.2011.01.056.
Full textGeorge, G. N., Y. Gea, R. C. Prince, S. Mukund, and M. W. W. Adams. "Tungsten oxo-thiolate enzymes from hyperthermophilic bacteria." Journal of Inorganic Biochemistry 43, no. 2-3 (August 1991): 241. http://dx.doi.org/10.1016/0162-0134(91)84231-w.
Full textScott, 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, and 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, no. 20 (August 14, 2015): 7339–47. http://dx.doi.org/10.1128/aem.01634-15.
Full textYang, Jing, John H. Enemark, and Martin L. Kirk. "Metal–Dithiolene Bonding Contributions to Pyranopterin Molybdenum Enzyme Reactivity." Inorganics 8, no. 3 (March 5, 2020): 19. http://dx.doi.org/10.3390/inorganics8030019.
Full textLeimkühler, Silke. "Metal-Containing Formate Dehydrogenases, a Personal View." Molecules 28, no. 14 (July 11, 2023): 5338. http://dx.doi.org/10.3390/molecules28145338.
Full textBrondino, Carlos D., Maria João Romão, Isabel Moura, and José JG Moura. "Molybdenum and tungsten enzymes: the xanthine oxidase family." Current Opinion in Chemical Biology 10, no. 2 (April 2006): 109–14. http://dx.doi.org/10.1016/j.cbpa.2006.01.034.
Full textHagen, Wilfred R. "The Development of Tungsten Biochemistry—A Personal Recollection." Molecules 28, no. 10 (May 11, 2023): 4017. http://dx.doi.org/10.3390/molecules28104017.
Full textSchulzke, Carola, and Christian Fischer. "Molybdenum and tungsten oxidoreductase model chemistry." Acta Crystallographica Section A Foundations and Advances 70, a1 (August 5, 2014): C1372. http://dx.doi.org/10.1107/s2053273314086276.
Full textSohail, Muhammad, Muhammad Zeshan Ashraf, Raziya Nadeem, Shamsa Bibi, Rabia Rehman, and Muhammad Adnan Iqbal. "Techniques in the synthesis of organometallic compounds of tungsten." Reviews in Inorganic Chemistry 40, no. 1 (March 26, 2020): 1–45. http://dx.doi.org/10.1515/revic-2019-0013.
Full textAkbassova, A., M. Beisekova, A. Tassanbiyeva, D. Zhamshitova, A. Kurmanbayeva, S. Zhangazin, N. Moldakimova, A. Shalabayeva, Zh Masalimov, and A. Akbassova. "COMBINED EFFECT OF TBSV P19 MUTANTS AND HEAVY METALS ON ANTIOXIDANT ENZYME ACTIVITY." Eurasian Journal of Applied Biotechnology, no. 3 (October 16, 2023): 48–59. http://dx.doi.org/10.11134/btp.3.2023.6.
Full textMukhamejanova, Akmaral, Zerekbay Alikulov, Bakyt Tuganova, and 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 (July 12, 2021): 632–38. http://dx.doi.org/10.5219/1665.
Full textRomão, Maria João. "Molybdenum and tungsten enzymes: a crystallographic and mechanistic overview." Dalton Transactions, no. 21 (2009): 4053. http://dx.doi.org/10.1039/b821108f.
Full textMcMaster, J., and John H. Enemark. "The active sites of molybdenum- and tungsten-containing enzymes." Current Opinion in Chemical Biology 2, no. 2 (April 1998): 201–7. http://dx.doi.org/10.1016/s1367-5931(98)80061-6.
Full textCordas, Cristina M., and José J. G. Moura. "Molybdenum and tungsten enzymes redox properties – A brief overview." Coordination Chemistry Reviews 394 (September 2019): 53–64. http://dx.doi.org/10.1016/j.ccr.2019.05.005.
Full textBoll, Matthias, Oliver Einsle, Ulrich Ermler, Peter M. H. Kroneck, and 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, no. 1-3 (2016): 119–37. http://dx.doi.org/10.1159/000440805.
Full textRoy, Roopali, Swarnalatha Mukund, Gerrit J. Schut, Dianne M. Dunn, Robert Weiss, and 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, no. 4 (February 15, 1999): 1171–80. http://dx.doi.org/10.1128/jb.181.4.1171-1180.1999.
Full textYergaliev, T. "Molybdenum and plant resistance to viral infection." BULLETIN of the L.N. Gumilyov Eurasian National University. BIOSCIENCE Series 135, no. 2 (2021): 63–70. http://dx.doi.org/10.32523/2616-7034-2021-135-2-63-70.
Full textMoura, José J. G., Paul V. Bernhardt, Luísa B. Maia, and Pablo J. Gonzalez. "Molybdenum and tungsten enzymes: from biology to chemistry and back." JBIC Journal of Biological Inorganic Chemistry 20, no. 2 (February 11, 2015): 181–82. http://dx.doi.org/10.1007/s00775-015-1243-9.
Full textRothery, R. A., B. Stein, M. Solomonson, M. L. Kirk, and J. H. Weiner. "Pyranopterin conformation defines the function of molybdenum and tungsten enzymes." Proceedings of the National Academy of Sciences 109, no. 37 (August 27, 2012): 14773–78. http://dx.doi.org/10.1073/pnas.1200671109.
Full textRoy, Roopali, and Michael W. W. Adams. "Characterization of a Fourth Tungsten-Containing Enzyme from the Hyperthermophilic Archaeon Pyrococcus furiosus." Journal of Bacteriology 184, no. 24 (December 15, 2002): 6952–56. http://dx.doi.org/10.1128/jb.184.24.6952-6956.2002.
Full textGrant, MP, CR VanderSchee, H. Chou, A. Bolt, LM Epure, D. Kuter, J. Antoniou, S. Bohle, KK Mann, and 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 (May 17, 2021): 517–30. http://dx.doi.org/10.22203/ecm.v041a33.
Full textBurgmayer, Sharon J. Nieter, and Martin L. Kirk. "Advancing Our Understanding of Pyranopterin-Dithiolene Contributions to Moco Enzyme Catalysis." Molecules 28, no. 22 (November 7, 2023): 7456. http://dx.doi.org/10.3390/molecules28227456.
Full textYoung, Charles G., and Anthony G. Wedd. "Metal chemistry relevant to the mononuclear molybdenum and tungsten pterin enzymes." Chemical Communications, no. 14 (1997): 1251–57. http://dx.doi.org/10.1039/a606660g.
Full textENEMARK, J. H., and C. G. YOUNG. "ChemInform Abstract: Bioinorganic Chemistry of Pterin-Containing Molybdenum and Tungsten Enzymes." ChemInform 25, no. 43 (August 18, 2010): no. http://dx.doi.org/10.1002/chin.199443309.
Full textSihombing, Victor H., and Abd Hakim S. "The Use of Tungsten in Potentiometry to Detect Pospat Baffer and Urease Enzyme." Jurnal Penelitian Pendidikan IPA 7, no. 3 (May 26, 2021): 325. http://dx.doi.org/10.29303/jppipa.v7i3.699.
Full textSugimoto, Hideki, and Kunihisa Sugimoto. "New bis(pyranodithiolene) tungsten(IV) and (VI) complexes as chemical analogues of the active sites of tungsten enzymes." Inorganic Chemistry Communications 11, no. 1 (January 2008): 77–80. http://dx.doi.org/10.1016/j.inoche.2007.10.020.
Full textS, 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 (December 26, 2021): 370–76. http://dx.doi.org/10.29303/jppipa.v7ispecialissue.1248.
Full textFogeron, Thibault, Yun Li, and Marc Fontecave. "Formate Dehydrogenase Mimics as Catalysts for Carbon Dioxide Reduction." Molecules 27, no. 18 (September 14, 2022): 5989. http://dx.doi.org/10.3390/molecules27185989.
Full textSosorova, S. B., I. N. Lavrent’eva, L. N. Boloneva, V. L. Ubugunov, and 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, no. 7 (July 20, 2021): 48–53. http://dx.doi.org/10.18412/1816-0395-2021-7-48-53.
Full textStiefel, E. I. "Transition metal sulfur chemistry and its relvance to molybdenum and tungsten enzymes." Journal of Inorganic Biochemistry 67, no. 1-4 (July 1997): 8. http://dx.doi.org/10.1016/s0162-0134(97)89891-1.
Full textMajumdar, Amit, and Sabyasachi Sarkar. "Bioinorganic chemistry of molybdenum and tungsten enzymes: A structural–functional modeling approach." Coordination Chemistry Reviews 255, no. 9-10 (May 2011): 1039–54. http://dx.doi.org/10.1016/j.ccr.2010.11.027.
Full textStiefel, E. I. "Transition metal sulfur chemistry and its relevance to molybdenum and tungsten enzymes." Pure and Applied Chemistry 70, no. 4 (January 1, 1998): 889–96. http://dx.doi.org/10.1351/pac199870040889.
Full textSerikovna, Tokasheva Dana, Akbassova Alya Zholdasbayevna, and 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, no. 1 (January 23, 2024): 261–70. http://dx.doi.org/10.53894/ijirss.v7i1.2616.
Full textPark, Myong-Ok, Taeko Mizutani, and Patrik R. Jones. "Glyceraldehyde-3-Phosphate Ferredoxin Oxidoreductase from Methanococcus maripaludis." Journal of Bacteriology 189, no. 20 (August 17, 2007): 7281–89. http://dx.doi.org/10.1128/jb.00828-07.
Full textJoshi, H. K., J. J. A. Cooney, F. E. Inscore, N. E. Gruhn, D. L. Lichtenberger, and J. H. Enemark. "Investigation of metal-dithiolate fold angle effects: Implications for molybdenum and tungsten enzymes." Proceedings of the National Academy of Sciences 100, no. 7 (March 24, 2003): 3719–24. http://dx.doi.org/10.1073/pnas.0636832100.
Full textYOUNG, C. G., and A. G. WEDD. "ChemInform Abstract: Metal Chemistry Relevant to the Mononuclear Molybdenum and Tungsten Pterin Enzymes." ChemInform 28, no. 42 (August 3, 2010): no. http://dx.doi.org/10.1002/chin.199742321.
Full textTokasheva, D. S., M. K. Beisekova, K. E. Zhanassova, Zh B. Tleukulova, A. Zh Akbasova, and 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, no. 4 (2021): 84–91. http://dx.doi.org/10.32523/2616-7034-2021-137-4-84-91.
Full textSugimoto, Hideki, Hiroyuki Tano, Reiko Tajima, Hiroyuki Miyake, Hiroshi Tsukube, Hiromi Ohi, and 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, no. 21 (October 2007): 8460–62. http://dx.doi.org/10.1021/ic7012733.
Full textHuwiler, Simona G., Claudia Löffler, Sebastian E. L. Anselmann, Hans-Joachim Stärk, Martin von Bergen, Jennifer Flechsler, Reinhard Rachel, and 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, no. 6 (January 23, 2019): 2259–64. http://dx.doi.org/10.1073/pnas.1819636116.
Full textBurgmayer, Sharon. "Making Moco: A Personal History." Molecules 28, no. 21 (October 27, 2023): 7296. http://dx.doi.org/10.3390/molecules28217296.
Full textMaia, Luisa B. "Bringing Nitric Oxide to the Molybdenum World—A Personal Perspective." Molecules 28, no. 15 (August 2, 2023): 5819. http://dx.doi.org/10.3390/molecules28155819.
Full textHolm, Richard H., Edward I. Solomon, Amit Majumdar, and Adam Tenderholt. "Comparative molecular chemistry of molybdenum and tungsten and its relation to hydroxylase and oxotransferase enzymes." Coordination Chemistry Reviews 255, no. 9-10 (May 2011): 993–1015. http://dx.doi.org/10.1016/j.ccr.2010.10.017.
Full textSugimoto, 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.
Full textPermyakov, Eugene A. "Metal Binding Proteins." Encyclopedia 1, no. 1 (March 15, 2021): 261–92. http://dx.doi.org/10.3390/encyclopedia1010024.
Full textHochheimer, Andreas, Ruth A. Schmitz, Rudolf K. Thauer, and Reiner Hedderich. "The Tungsten Formylmethanofuran Dehydrogenase from Methanobacterium Thermoautotrophicum Contains Sequence Motifs Characteristic for Enzymes Containing Molybdopterin Dinucleotide." European Journal of Biochemistry 234, no. 3 (December 1995): 910–20. http://dx.doi.org/10.1111/j.1432-1033.1995.910_a.x.
Full textSugimoto, Hideki, Kohei Hatakeda, Kazuo Toyota, Susumu Tatemoto, Minoru Kubo, Takashi Ogura, and 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, no. 9 (2013): 3059–70. http://dx.doi.org/10.1039/c2dt32179c.
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