Artigos de revistas sobre o tema "Copper monooxygenases"
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Fukatsu, Arisa, Yuma Morimoto, Hideki Sugimoto e Shinobu Itoh. "Modelling a ‘histidine brace’ motif in mononuclear copper monooxygenases". Chemical Communications 56, n.º 38 (2020): 5123–26. http://dx.doi.org/10.1039/d0cc01392g.
Texto completo da fonteMusiani, Francesco, Valquiria Broll, Elisa Evangelisti e Stefano Ciurli. "The model structure of the copper-dependent ammonia monooxygenase". JBIC Journal of Biological Inorganic Chemistry 25, n.º 7 (14 de setembro de 2020): 995–1007. http://dx.doi.org/10.1007/s00775-020-01820-0.
Texto completo da fonteLiew, Elissa F., Daochen Tong, Nicholas V. Coleman e Andrew J. Holmes. "Mutagenesis of the hydrocarbon monooxygenase indicates a metal centre in subunit-C, and not subunit-B, is essential for copper-containing membrane monooxygenase activity". Microbiology 160, n.º 6 (1 de junho de 2014): 1267–77. http://dx.doi.org/10.1099/mic.0.078584-0.
Texto completo da fonteFarhan Ul Haque, Muhammad, Bhagyalakshmi Kalidass, Nathan Bandow, Erick A. Turpin, Alan A. DiSpirito e Jeremy D. Semrau. "Cerium Regulates Expression of Alternative Methanol Dehydrogenases in Methylosinus trichosporium OB3b". Applied and Environmental Microbiology 81, n.º 21 (21 de agosto de 2015): 7546–52. http://dx.doi.org/10.1128/aem.02542-15.
Texto completo da fonteVu, Van V., e Son Tung Ngo. "Copper active site in polysaccharide monooxygenases". Coordination Chemistry Reviews 368 (agosto de 2018): 134–57. http://dx.doi.org/10.1016/j.ccr.2018.04.005.
Texto completo da fonteBlackburn, Ninian J., Brian Reedy, Eilleen Zhou, Robert Carr e Steven J. Benkovic. "Chemistry and spectroscopy of copper monooxygenases". Journal of Inorganic Biochemistry 47, n.º 3-4 (julho de 1992): 8. http://dx.doi.org/10.1016/0162-0134(92)84079-3.
Texto completo da fonteChoi, Dong-W., Ryan C. Kunz, Eric S. Boyd, Jeremy D. Semrau, William E. Antholine, J. I. Han, James A. Zahn, Jeffrey M. Boyd, Arlene M. de la Mora e Alan A. DiSpirito. "The Membrane-Associated Methane Monooxygenase (pMMO) and pMMO-NADH:Quinone Oxidoreductase Complex from Methylococcus capsulatus Bath". Journal of Bacteriology 185, n.º 19 (1 de outubro de 2003): 5755–64. http://dx.doi.org/10.1128/jb.185.19.5755-5764.2003.
Texto completo da fonteHedegård, Erik Donovan, e Ulf Ryde. "Molecular mechanism of lytic polysaccharide monooxygenases". Chemical Science 9, n.º 15 (2018): 3866–80. http://dx.doi.org/10.1039/c8sc00426a.
Texto completo da fonteItoh, Shinobu, e Shunichi Fukuzumi. "Dioxygen Activation by Copper Complexes. Mechanistic Insights into Copper Monooxygenases and Copper Oxidases". Bulletin of the Chemical Society of Japan 75, n.º 10 (outubro de 2002): 2081–95. http://dx.doi.org/10.1246/bcsj.75.2081.
Texto completo da fonteMaiti, Debabrata, Amy A. Narducci Sarjeant e Kenneth D. Karlin. "Copper−Hydroperoxo-Mediated N-Debenzylation Chemistry Mimicking Aspects of Copper Monooxygenases". Inorganic Chemistry 47, n.º 19 (6 de outubro de 2008): 8736–47. http://dx.doi.org/10.1021/ic800617m.
Texto completo da fonteFujisawa, K., T. Katayama, N. Kitajima e Y. Moro-oka. "Reaction aspects of peroxo copper complexes relevant to copper containing monooxygenases." Journal of Inorganic Biochemistry 43, n.º 2-3 (agosto de 1991): 216. http://dx.doi.org/10.1016/0162-0134(91)84208-q.
Texto completo da fonteMigliore, Agostino, e David N. Beratan. "Cu-To-Cu Electron Tunneling in Copper Monooxygenases". Biophysical Journal 106, n.º 2 (janeiro de 2014): 588a. http://dx.doi.org/10.1016/j.bpj.2013.11.3259.
Texto completo da fonteCiano, Luisa, Alessandro Paradisi, Glyn R. Hemsworth, Morten Tovborg, Gideon J. Davies e Paul H. Walton. "Insights from semi-oriented EPR spectroscopy studies into the interaction of lytic polysaccharide monooxygenases with cellulose". Dalton Transactions 49, n.º 11 (2020): 3413–22. http://dx.doi.org/10.1039/c9dt04065j.
Texto completo da fonteITO, M., K. FUJISAWA, N. KITAJIMA e Y. MORO-OKA. "ChemInform Abstract: Model Studies on Nonheme Monooxygenases. Chemical Models for Nonheme Iron and Copper Monooxygenases". ChemInform 28, n.º 28 (3 de agosto de 2010): no. http://dx.doi.org/10.1002/chin.199728284.
Texto completo da fonteBissaro, Bastien, e Vincent G. H. Eijsink. "Lytic polysaccharide monooxygenases: enzymes for controlled and site-specific Fenton-like chemistry". Essays in Biochemistry 67, n.º 3 (março de 2023): 575–84. http://dx.doi.org/10.1042/ebc20220250.
Texto completo da fonteMurrell, J. Colin, Ian R. McDonald e Bettina Gilbert. "Regulation of expression of methane monooxygenases by copper ions". Trends in Microbiology 8, n.º 5 (maio de 2000): 221–25. http://dx.doi.org/10.1016/s0966-842x(00)01739-x.
Texto completo da fonteConcia, Alda Lisa, Maria Rosa Beccia, Maylis Orio, Francine Terra Ferre, Marciela Scarpellini, Frédéric Biaso, Bruno Guigliarelli, Marius Réglier e A. Jalila Simaan. "Copper Complexes as Bioinspired Models for Lytic Polysaccharide Monooxygenases". Inorganic Chemistry 56, n.º 3 (6 de janeiro de 2017): 1023–26. http://dx.doi.org/10.1021/acs.inorgchem.6b02165.
Texto completo da fonteBeeson, William T., Christopher M. Phillips, Jamie H. D. Cate e Michael A. Marletta. "Oxidative Cleavage of Cellulose by Fungal Copper-Dependent Polysaccharide Monooxygenases". Journal of the American Chemical Society 134, n.º 2 (28 de dezembro de 2011): 890–92. http://dx.doi.org/10.1021/ja210657t.
Texto completo da fonteNgo, Son Tung, Han N. Phan, Chinh N. Le, Nhung C. T. Ngo, Khanh Bao Vu, Nguyen Thanh Tung, Cuong X. Luu e Van V. Vu. "Fine Tuning of the Copper Active Site in Polysaccharide Monooxygenases". Journal of Physical Chemistry B 124, n.º 10 (28 de janeiro de 2020): 1859–65. http://dx.doi.org/10.1021/acs.jpcb.9b08114.
Texto completo da fonteBogush, T. A., F. V. Donenko, S. M. Sitdikova e N. V. Andronova. "Interaction of the copper complex Cu-2 with liver monooxygenases". Bulletin of Experimental Biology and Medicine 104, n.º 4 (outubro de 1987): 1394–96. http://dx.doi.org/10.1007/bf00834954.
Texto completo da fonteHamamura, Natsuko, Chris M. Yeager e Daniel J. Arp. "Two Distinct Monooxygenases for Alkane Oxidation inNocardioides sp. Strain CF8". Applied and Environmental Microbiology 67, n.º 11 (1 de novembro de 2001): 4992–98. http://dx.doi.org/10.1128/aem.67.11.4992-4998.2001.
Texto completo da fonteBissaro, Bastien, Bennett Streit, Ingvild Isaksen, Vincent G. H. Eijsink, Gregg T. Beckham, Jennifer L. DuBois e Åsmund K. Røhr. "Molecular mechanism of the chitinolytic peroxygenase reaction". Proceedings of the National Academy of Sciences 117, n.º 3 (6 de janeiro de 2020): 1504–13. http://dx.doi.org/10.1073/pnas.1904889117.
Texto completo da fonteMerkler, David J., Raviraj Kulathila, Wilson A. Francisco, David E. Ash e Joseph Bell. "The irreversible inactivation of two copper-dependent monooxygenases by sulfite: peptidylglycine α-amidating enzyme and dopamine β-monooxygenase". FEBS Letters 366, n.º 2-3 (12 de junho de 1995): 165–69. http://dx.doi.org/10.1016/0014-5793(95)00516-c.
Texto completo da fonteCowley, Ryan E., Li Tian e Edward I. Solomon. "Mechanism of O2 activation and substrate hydroxylation in noncoupled binuclear copper monooxygenases". Proceedings of the National Academy of Sciences 113, n.º 43 (10 de outubro de 2016): 12035–40. http://dx.doi.org/10.1073/pnas.1614807113.
Texto completo da fonteTandrup, Tobias, Kristian E. H. Frandsen, Katja S. Johansen, Jean-Guy Berrin e Leila Lo Leggio. "Recent insights into lytic polysaccharide monooxygenases (LPMOs)". Biochemical Society Transactions 46, n.º 6 (31 de outubro de 2018): 1431–47. http://dx.doi.org/10.1042/bst20170549.
Texto completo da fonteRochman, Fauziah F., Miye Kwon, Roshan Khadka, Ivica Tamas, Azriel Abraham Lopez-Jauregui, Andriy Sheremet, Angela V. Smirnova et al. "Novel copper-containing membrane monooxygenases (CuMMOs) encoded by alkane-utilizing Betaproteobacteria". ISME Journal 14, n.º 3 (3 de dezembro de 2019): 714–26. http://dx.doi.org/10.1038/s41396-019-0561-2.
Texto completo da fonteSabbadin, Federico, Saioa Urresti, Bernard Henrissat, Anna O. Avrova, Lydia R. J. Welsh, Peter J. Lindley, Michael Csukai et al. "Secreted pectin monooxygenases drive plant infection by pathogenic oomycetes". Science 373, n.º 6556 (12 de agosto de 2021): 774–79. http://dx.doi.org/10.1126/science.abj1342.
Texto completo da fonteLiu, Yucui, Wei Ma e Xu Fang. "The Role of the Residue at Position 2 in the Catalytic Activity of AA9 Lytic Polysaccharide Monooxygenases". International Journal of Molecular Sciences 24, n.º 9 (5 de maio de 2023): 8300. http://dx.doi.org/10.3390/ijms24098300.
Texto completo da fontePrigge, S. T., R. E. Mains, B. A. Eipper e L. M. Amzel* **. "New insights into copper monooxygenases and peptide amidation: structure, mechanism and function". Cellular and Molecular Life Sciences 57, n.º 8 (agosto de 2000): 1236–59. http://dx.doi.org/10.1007/pl00000763.
Texto completo da fonteItoh, Shinobu. "Dioxygen activation by copper complexes supported by 2-(2-pyridyl)ethylamine ligands. Mechanistic insights into copper monooxygenases and copper oxidases". Journal of Inorganic Biochemistry 96, n.º 1 (julho de 2003): 20. http://dx.doi.org/10.1016/s0162-0134(03)80437-3.
Texto completo da fonteIpsen, Johan Ø., Magnus Hallas-Møller, Søren Brander, Leila Lo Leggio e Katja S. Johansen. "Lytic polysaccharide monooxygenases and other histidine-brace copper proteins: structure, oxygen activation and biotechnological applications". Biochemical Society Transactions 49, n.º 1 (15 de janeiro de 2021): 531–40. http://dx.doi.org/10.1042/bst20201031.
Texto completo da fonteN. Le, Chinh, Cuong X. Luu, Son Tung Ngo e Van V. Vu. "DFT studies of the copper active site in AA13 polysaccharide monooxygenase". Ministry of Science and Technology, Vietnam 64, n.º 4 (15 de dezembro de 2022): 28–31. http://dx.doi.org/10.31276/vjste.64(4).28-31.
Texto completo da fonteCourtade, Gaston, Reinhard Wimmer, Åsmund K. Røhr, Marita Preims, Alfons K. G. Felice, Maria Dimarogona, Gustav Vaaje-Kolstad et al. "Interactions of a fungal lytic polysaccharide monooxygenase with β-glucan substrates and cellobiose dehydrogenase". Proceedings of the National Academy of Sciences 113, n.º 21 (5 de maio de 2016): 5922–27. http://dx.doi.org/10.1073/pnas.1602566113.
Texto completo da fonteBlain, Ingrid, Patrick Slama, Michel Giorgi, Thierry Tron e Marius Réglier. "Copper-containing monooxygenases: enzymatic and biomimetic studies of the O-atom transfer catalysis". Reviews in Molecular Biotechnology 90, n.º 2 (abril de 2002): 95–112. http://dx.doi.org/10.1016/s1389-0352(01)00068-x.
Texto completo da fonteFilandr, Frantisek, Daniel Kavan, Daniel Kracher, Christophe V. F. P. Laurent, Roland Ludwig, Petr Man e Petr Halada. "Structural Dynamics of Lytic Polysaccharide Monooxygenase during Catalysis". Biomolecules 10, n.º 2 (5 de fevereiro de 2020): 242. http://dx.doi.org/10.3390/biom10020242.
Texto completo da fonteItoh, Shinobu, Hajime Nakao e Shunichi Fukuzumi. "Mechanistic studies of aliphatic ligand hydroxylation of a copper complex by dioxygen: A model reaction for copper monooxygenases". Journal of Inorganic Biochemistry 67, n.º 1-4 (julho de 1997): 65. http://dx.doi.org/10.1016/s0162-0134(97)89946-1.
Texto completo da fonteItoh, Shinobu, Hajime Nakao, Lisa M. Berreau, Toshihiko Kondo, Mitsuo Komatsu e Shunichi Fukuzumi. "Mechanistic Studies of Aliphatic Ligand Hydroxylation of a Copper Complex by Dioxygen: A Model Reaction for Copper Monooxygenases". Journal of the American Chemical Society 120, n.º 12 (abril de 1998): 2890–99. http://dx.doi.org/10.1021/ja972809q.
Texto completo da fonteIvanova, Anastasia A., Igor Y. Oshkin, Olga V. Danilova, Dmitriy A. Philippov, Nikolai V. Ravin e Svetlana N. Dedysh. "Rokubacteria in Northern Peatlands: Habitat Preferences and Diversity Patterns". Microorganisms 10, n.º 1 (22 de dezembro de 2021): 11. http://dx.doi.org/10.3390/microorganisms10010011.
Texto completo da fonteSchicke, Olivier, Bruno Faure, Yannick Carissan, Michel Giorgi, Ariane Jalila Simaan e Marius Réglier. "Synthesis and Characterization of a Dinuclear Copper Complex Bearing a Hydrophobic Cavity as a Model for Copper-Containing Monooxygenases". European Journal of Inorganic Chemistry 2015, n.º 21 (3 de junho de 2015): 3512–18. http://dx.doi.org/10.1002/ejic.201500280.
Texto completo da fonteAyub, Hina, Min-Ju Kang, Adeel Farooq e Man-Young Jung. "Ecological Aerobic Ammonia and Methane Oxidation Involved Key Metal Compounds, Fe and Cu". Life 12, n.º 11 (7 de novembro de 2022): 1806. http://dx.doi.org/10.3390/life12111806.
Texto completo da fonteBranch, Jessie, Badri S. Rajagopal, Alessandro Paradisi, Nick Yates, Peter J. Lindley, Jake Smith, Kristian Hollingsworth et al. "C-type cytochrome-initiated reduction of bacterial lytic polysaccharide monooxygenases". Biochemical Journal 478, n.º 14 (28 de julho de 2021): 2927–44. http://dx.doi.org/10.1042/bcj20210376.
Texto completo da fonteSvenning, Mette M., Anne Grethe Hestnes, Ingvild Wartiainen, Lisa Y. Stein, Martin G. Klotz, Marina G. Kalyuzhnaya, Anja Spang et al. "Genome Sequence of the Arctic Methanotroph Methylobacter tundripaludum SV96". Journal of Bacteriology 193, n.º 22 (1 de julho de 2011): 6418–19. http://dx.doi.org/10.1128/jb.05380-11.
Texto completo da fonteSamanta, Dipayan, Tanvi Govil, Priya Saxena, Lee Krumholz, Venkataramana Gadhamshetty, Kian Mau Goh e Rajesh K. Sani. "Genetical and Biochemical Basis of Methane Monooxygenases of Methylosinus trichosporium OB3b in Response to Copper". Methane 3, n.º 1 (20 de fevereiro de 2024): 103–21. http://dx.doi.org/10.3390/methane3010007.
Texto completo da fonteFrandsen, Kristian E. H., e Leila Lo Leggio. "Lytic polysaccharide monooxygenases: a crystallographer's view on a new class of biomass-degrading enzymes". IUCrJ 3, n.º 6 (14 de outubro de 2016): 448–67. http://dx.doi.org/10.1107/s2052252516014147.
Texto completo da fonteWu, Peng, Fangfang Fan, Jinshuai Song, Wei Peng, Jia Liu, Chunsen Li, Zexing Cao e Binju Wang. "Theory Demonstrated a “Coupled” Mechanism for O2 Activation and Substrate Hydroxylation by Binuclear Copper Monooxygenases". Journal of the American Chemical Society 141, n.º 50 (20 de novembro de 2019): 19776–89. http://dx.doi.org/10.1021/jacs.9b09172.
Texto completo da fonteKim, S., J. Stahlberg, M. Sandgren, R. S. Paton e G. T. Beckham. "Quantum mechanical calculations suggest that lytic polysaccharide monooxygenases use a copper-oxyl, oxygen-rebound mechanism". Proceedings of the National Academy of Sciences 111, n.º 1 (16 de dezembro de 2013): 149–54. http://dx.doi.org/10.1073/pnas.1316609111.
Texto completo da fonteSchröder, Gabriela C., William B. O'Dell, Paul D. Swartz e Flora Meilleur. "Preliminary results of neutron and X-ray diffraction data collection on a lytic polysaccharide monooxygenase under reduced and acidic conditions". Acta Crystallographica Section F Structural Biology Communications 77, n.º 4 (31 de março de 2021): 128–33. http://dx.doi.org/10.1107/s2053230x21002399.
Texto completo da fonteCastillo, Ivan, Andrea C. Neira, Ebbe Nordlander e Erica Zeglio. "Bis(benzimidazolyl)amine copper complexes with a synthetic ‘histidine brace’ structural motif relevant to polysaccharide monooxygenases". Inorganica Chimica Acta 422 (outubro de 2014): 152–57. http://dx.doi.org/10.1016/j.ica.2014.06.027.
Texto completo da fonteXing, Zhilin, Tiantao Zhao, Lijie Zhang, Yanhui Gao, Shuai Liu e Xu Yang. "Effects of copper on expression of methane monooxygenases, trichloroethylene degradation, and community structure in methanotrophic consortia". Engineering in Life Sciences 18, n.º 4 (22 de fevereiro de 2018): 236–43. http://dx.doi.org/10.1002/elsc.201700153.
Texto completo da fonteNaik, Anil D., Pattubala A. N. Reddy, Munirathinam Nethaji e Akhil R. Chakravarty. "Ternary copper(II) complexes of thiosemicarbazones and heterocyclic bases showing N3OS coordination as models for the type-2 centers of copper monooxygenases". Inorganica Chimica Acta 349 (junho de 2003): 149–58. http://dx.doi.org/10.1016/s0020-1693(03)00091-4.
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