Статті в журналах з теми "Peroxygenase activity"
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Zámocký, Marcel, and Jana Harichová. "Evolution of Heme Peroxygenases: Ancient Roots and Later Evolved Branches." Antioxidants 11, no. 5 (May 20, 2022): 1011. http://dx.doi.org/10.3390/antiox11051011.
Повний текст джерелаWillot, Tieves, Girhard, Urlacher, Hollmann, and de Gonzalo. "P450BM3-Catalyzed Oxidations Employing Dual Functional Small Molecules." Catalysts 9, no. 7 (June 26, 2019): 567. http://dx.doi.org/10.3390/catal9070567.
Повний текст джерелаKuo, H. H., and A. G. Mauk. "Indole peroxygenase activity of indoleamine 2,3-dioxygenase." Proceedings of the National Academy of Sciences 109, no. 35 (August 13, 2012): 13966–71. http://dx.doi.org/10.1073/pnas.1207191109.
Повний текст джерелаHanano, Abdulsamie, Ibrahem Almousally, Mouhnad Shaban, and Elizabeth Blee. "A Caleosin-Like Protein with Peroxygenase Activity Mediates Aspergillus flavus Development, Aflatoxin Accumulation, and Seed Infection." Applied and Environmental Microbiology 81, no. 18 (June 26, 2015): 6129–44. http://dx.doi.org/10.1128/aem.00867-15.
Повний текст джерелаNguyen, Thi, Soo-Jin Yeom, and Chul-Ho Yun. "Production of a Human Metabolite of Atorvastatin by Bacterial CYP102A1 Peroxygenase." Applied Sciences 11, no. 2 (January 10, 2021): 603. http://dx.doi.org/10.3390/app11020603.
Повний текст джерелаNguyen, Thi Huong Ha, Soo-Jin Yeom, and Chul-Ho Yun. "Production of a Human Metabolite of Atorvastatin by Bacterial CYP102A1 Peroxygenase." Applied Sciences 11, no. 2 (January 10, 2021): 603. http://dx.doi.org/10.3390/app11020603.
Повний текст джерелаMolina-Espeja, Patricia, Eva Garcia-Ruiz, David Gonzalez-Perez, René Ullrich, Martin Hofrichter, and Miguel Alcalde. "Directed Evolution of Unspecific Peroxygenase from Agrocybe aegerita." Applied and Environmental Microbiology 80, no. 11 (March 28, 2014): 3496–507. http://dx.doi.org/10.1128/aem.00490-14.
Повний текст джерелаMolina-Espeja, Patricia, Paloma Santos-Moriano, Eva García-Ruiz, Antonio Ballesteros, Francisco Plou, and Miguel Alcalde. "Structure-Guided Immobilization of an Evolved Unspecific Peroxygenase." International Journal of Molecular Sciences 20, no. 7 (April 2, 2019): 1627. http://dx.doi.org/10.3390/ijms20071627.
Повний текст джерелаQin, Xiangquan, Yiping Jiang, Jie Chen, Fuquan Yao, Panxia Zhao, Longyi Jin, and Zhiqi Cong. "Co-Crystal Structure-Guided Optimization of Dual-Functional Small Molecules for Improving the Peroxygenase Activity of Cytochrome P450BM3." International Journal of Molecular Sciences 23, no. 14 (July 18, 2022): 7901. http://dx.doi.org/10.3390/ijms23147901.
Повний текст джерелаCarballares, Diego, Roberto Morellon-Sterling, Xiaomin Xu, Frank Hollmann, and Roberto Fernandez-Lafuente. "Immobilization of the Peroxygenase from Agrocybe aegerita. The Effect of the Immobilization pH on the Features of an Ionically Exchanged Dimeric Peroxygenase." Catalysts 11, no. 5 (April 28, 2021): 560. http://dx.doi.org/10.3390/catal11050560.
Повний текст джерелаSanchez-Sanchez, Lorena, Rosa Roman, and Rafael Vazquez-Duhalt. "Pesticide transformation by a variant of CYPBM3 with improved peroxygenase activity." Pesticide Biochemistry and Physiology 102, no. 2 (February 2012): 169–74. http://dx.doi.org/10.1016/j.pestbp.2011.12.010.
Повний текст джерелаMcCombs, Nikolette L., Jennifer D’Antonio, David A. Barrios, Leiah M. Carey, and Reza A. Ghiladi. "Nonmicrobial Nitrophenol Degradation via Peroxygenase Activity of Dehaloperoxidase-Hemoglobin fromAmphitrite ornata." Biochemistry 55, no. 17 (April 22, 2016): 2465–78. http://dx.doi.org/10.1021/acs.biochem.6b00143.
Повний текст джерелаRamirez-Ramirez, Joaquin, Javier Martin-Diaz, Nina Pastor, Miguel Alcalde, and Marcela Ayala. "Exploring the Role of Phenylalanine Residues in Modulating the Flexibility and Topography of the Active Site in the Peroxygenase Variant PaDa-I." International Journal of Molecular Sciences 21, no. 16 (August 10, 2020): 5734. http://dx.doi.org/10.3390/ijms21165734.
Повний текст джерелаSchramm, Marina, Stephanie Friedrich, Kai-Uwe Schmidtke, Jan Kiebist, Paul Panzer, Harald Kellner, René Ullrich, Martin Hofrichter, and Katrin Scheibner. "Cell-Free Protein Synthesis with Fungal Lysates for the Rapid Production of Unspecific Peroxygenases." Antioxidants 11, no. 2 (January 30, 2022): 284. http://dx.doi.org/10.3390/antiox11020284.
Повний текст джерелаBreslmayr, Erik, Peter Poliak, Alen Požgajčić, Roman Schindler, Daniel Kracher, Chris Oostenbrink, and Roland Ludwig. "Inhibition of the Peroxygenase Lytic Polysaccharide Monooxygenase by Carboxylic Acids and Amino Acids." Antioxidants 11, no. 6 (May 31, 2022): 1096. http://dx.doi.org/10.3390/antiox11061096.
Повний текст джерелаHayashi, Takashi, Takaaki Matsuda, and Yoshio Hisaeda. "Enhancement of Peroxygenase Activity of Horse Heart Myoglobin by Modification of Heme-propionate Side Chains." Chemistry Letters 32, no. 6 (June 2003): 496–97. http://dx.doi.org/10.1246/cl.2003.496.
Повний текст джерелаErman, James E., Heather Kilheeney, Anil K. Bidwai, Caitlan E. Ayala, and Lidia B. Vitello. "Peroxygenase activity of cytochrome c peroxidase and three apolar distal heme pocket mutants: hydroxylation of 1-methoxynaphthalene." BMC Biochemistry 14, no. 1 (2013): 19. http://dx.doi.org/10.1186/1471-2091-14-19.
Повний текст джерелаSavenkova, Marina I., Jane M. Kuo, and Paul R. Ortiz de Montellano. "Improvement of Peroxygenase Activity by Relocation of a Catalytic Histidine within the Active Site of Horseradish Peroxidase." Biochemistry 37, no. 30 (July 1998): 10828–36. http://dx.doi.org/10.1021/bi9725780.
Повний текст джерелаMireles, Raul, Joaquin Ramirez-Ramirez, Miguel Alcalde, and Marcela Ayala. "Ether Oxidation by an Evolved Fungal Heme-Peroxygenase: Insights into Substrate Recognition and Reactivity." Journal of Fungi 7, no. 8 (July 28, 2021): 608. http://dx.doi.org/10.3390/jof7080608.
Повний текст джерелаPodgorski, Matthew N., Joshua S. Harbort, Joel H. Z. Lee, Giang T. H. Nguyen, John B. Bruning, William A. Donald, Paul V. Bernhardt, Jeffrey R. Harmer, and Stephen G. Bell. "An Altered Heme Environment in an Engineered Cytochrome P450 Enzyme Enables the Switch from Monooxygenase to Peroxygenase Activity." ACS Catalysis 12, no. 3 (January 12, 2022): 1614–25. http://dx.doi.org/10.1021/acscatal.1c05877.
Повний текст джерелаMcGuire, Ashlyn H., Leiah M. Carey, Vesna de Serrano, Safaa Dali, and Reza A. Ghiladi. "Peroxidase versus Peroxygenase Activity: Substrate Substituent Effects as Modulators of Enzyme Function in the Multifunctional Catalytic Globin Dehaloperoxidase." Biochemistry 57, no. 30 (June 27, 2018): 4455–68. http://dx.doi.org/10.1021/acs.biochem.8b00540.
Повний текст джерелаDezvarei, Shaghayegh, Osami Shoji, Yoshihito Watanabe, and Stephen G. Bell. "The effect of decoy molecules on the activity of the P450Bm3 holoenzyme and a heme domain peroxygenase variant." Catalysis Communications 124 (May 2019): 97–102. http://dx.doi.org/10.1016/j.catcom.2019.03.004.
Повний текст джерелаCiaramella, Alberto, Gianluca Catucci, Gianfranco Gilardi, and Giovanna Di Nardo. "Crystal structure of bacterial CYP116B5 heme domain: New insights on class VII P450s structural flexibility and peroxygenase activity." International Journal of Biological Macromolecules 140 (November 2019): 577–87. http://dx.doi.org/10.1016/j.ijbiomac.2019.08.141.
Повний текст джерелаCirino, Patrick C., Yi Tang, Katsuyuki Takahashi, David A. Tirrell, and Frances H. Arnold. "Global incorporation of norleucine in place of methionine in cytochrome P450 BM-3 heme domain increases peroxygenase activity." Biotechnology and Bioengineering 83, no. 6 (July 24, 2003): 729–34. http://dx.doi.org/10.1002/bit.10718.
Повний текст джерелаWei, Xiaoyao, Chun Zhang, Xiaowei Gao, Yanping Gao, Ya Yang, Kai Guo, Xi Du, Lin Pu, and Qin Wang. "Enhanced Activity and Substrate Specificity by Site‐Directed Mutagenesis for the P450 119 Peroxygenase Catalyzed Sulfoxidation of Thioanisole." ChemistryOpen 8, no. 8 (July 2, 2019): 1076–83. http://dx.doi.org/10.1002/open.201900157.
Повний текст джерелаLi, Maosheng, Hengmin Miao, Yanqing Li, Fang Wang, and Jiakun Xu. "Protein Engineering of an Artificial P450BM3 Peroxygenase System Enables Highly Selective O-Demethylation of Lignin Monomers." Molecules 27, no. 10 (May 13, 2022): 3120. http://dx.doi.org/10.3390/molecules27103120.
Повний текст джерелаHayashi, Takashi, Hideaki Sato, Takashi Matsuo, Takaaki Matsuda, Yutaka Hitomi, and Yoshio Hisaeda. "Enhancement of enzymatic activity for myoglobins by modification of heme-propionate side chains." Journal of Porphyrins and Phthalocyanines 08, no. 03 (March 2004): 255–64. http://dx.doi.org/10.1142/s1088424604000246.
Повний текст джерелаHlavica, P., I. Golly, M. Lehnerer, and J. Schulze. "Primary aromatic amines: their N-oxidative bioactivation." Human & Experimental Toxicology 16, no. 8 (August 1997): 441–48. http://dx.doi.org/10.1177/096032719701600805.
Повний текст джерелаDíaz-Quintana, Antonio, Gonzalo Pérez-Mejías, Alejandra Guerra-Castellano, Miguel A. De la Rosa, and Irene Díaz-Moreno. "Wheel and Deal in the Mitochondrial Inner Membranes: The Tale of Cytochrome c and Cardiolipin." Oxidative Medicine and Cellular Longevity 2020 (April 22, 2020): 1–20. http://dx.doi.org/10.1155/2020/6813405.
Повний текст джерелаHangasky, John A., Anthony T. Iavarone, and Michael A. Marletta. "Reactivity of O2 versus H2O2 with polysaccharide monooxygenases." Proceedings of the National Academy of Sciences 115, no. 19 (April 23, 2018): 4915–20. http://dx.doi.org/10.1073/pnas.1801153115.
Повний текст джерелаShen, Yue, Qing-Li Jia, Ming-Zhe Liu, Zhuo-Wei Li, Li-Li Wang, Cui-Zhu Zhao, Zhi-Xi Li, and Meng Zhang. "Genome-wide characterization and phylogenetic and expression analyses of the caleosin gene family in soybean, common bean and barrel medic." Archives of Biological Sciences 68, no. 3 (2016): 575–85. http://dx.doi.org/10.2298/abs150916048s.
Повний текст джерелаMatsuo, Takashi, and Takashi Hayashi. "Electron transfer and oxidase activities in reconstituted hemoproteins with chemically modified cofactors." Journal of Porphyrins and Phthalocyanines 13, no. 10 (October 2009): 1082–89. http://dx.doi.org/10.1142/s1088424609001340.
Повний текст джерелаLappe, Alessa, Nina Jankowski, Annemie Albrecht, and Katja Koschorreck. "Characterization of a thermotolerant aryl-alcohol oxidase from Moesziomyces antarcticus oxidizing 5-hydroxymethyl-2-furancarboxylic acid." Applied Microbiology and Biotechnology 105, no. 21-22 (October 13, 2021): 8313–27. http://dx.doi.org/10.1007/s00253-021-11557-8.
Повний текст джерелаAnh, Dau Hung, René Ullrich, Dirk Benndorf, Aleś Svatoś, Alexander Muck, and Martin Hofrichter. "The Coprophilous Mushroom Coprinus radians Secretes a Haloperoxidase That Catalyzes Aromatic Peroxygenation." Applied and Environmental Microbiology 73, no. 17 (June 29, 2007): 5477–85. http://dx.doi.org/10.1128/aem.00026-07.
Повний текст джерелаEbner, Katharina, Lukas J. Pfeifenberger, Claudia Rinnofner, Veronika Schusterbauer, Anton Glieder, and Margit Winkler. "Discovery and Heterologous Expression of Unspecific Peroxygenases." Catalysts 13, no. 1 (January 16, 2023): 206. http://dx.doi.org/10.3390/catal13010206.
Повний текст джерелаChen, Zhifeng, Jie Chen, Nana Ma, Haifeng Zhou, and Zhiqi Cong. "Selective hydroxylation of naphthalene using the H2O2-dependent engineered P450BM3 driven by dual-functional small molecules." Journal of Porphyrins and Phthalocyanines 22, no. 09n10 (August 21, 2018): 831–36. http://dx.doi.org/10.1142/s108842461850061x.
Повний текст джерелаPickl, Mathias, Sara Kurakin, Fabián G. Cantú Reinhard, Philipp Schmid, Alexander Pöcheim, Christoph K. Winkler, Wolfgang Kroutil, Sam P. de Visser, and Kurt Faber. "Mechanistic Studies of Fatty Acid Activation by CYP152 Peroxygenases Reveal Unexpected Desaturase Activity." ACS Catalysis 9, no. 1 (December 6, 2018): 565–77. http://dx.doi.org/10.1021/acscatal.8b03733.
Повний текст джерелаKarich, Alexander, Katrin Scheibner, René Ullrich, and Martin Hofrichter. "Exploring the catalase activity of unspecific peroxygenases and the mechanism of peroxide-dependent heme destruction." Journal of Molecular Catalysis B: Enzymatic 134 (December 2016): 238–46. http://dx.doi.org/10.1016/j.molcatb.2016.10.014.
Повний текст джерелаCho, Won-Il, and Myong-Soo Chung. "Bacillus spores: a review of their properties and inactivation processing technologies." Food Science and Biotechnology 29, no. 11 (October 6, 2020): 1447–61. http://dx.doi.org/10.1007/s10068-020-00809-4.
Повний текст джерелаCantú Reinhard, Fabián G., Yen-Ting Lin, Agnieszka Stańczak, and Sam P. de Visser. "Bioengineering of Cytochrome P450 OleTJE: How Does Substrate Positioning Affect the Product Distributions?" Molecules 25, no. 11 (June 9, 2020): 2675. http://dx.doi.org/10.3390/molecules25112675.
Повний текст джерелаGjorgjeska, Biljana, and Dino Karpicarov. "MECHANISM OF ACTION AND CHARACTERISTICS OF CERTAIN ANTISEPTICS AND DISINFECTANTS IN CORRELATION WITH THEIR ACTIVITY ON SELECTED MICROORGANISMS." Knowledge International Journal 28, no. 2 (December 10, 2018): 423–28. http://dx.doi.org/10.35120/kij2802423g.
Повний текст джерелаKont, Riin, Bastien Bissaro, Vincent G. H. Eijsink, and Priit Väljamäe. "Kinetic insights into the peroxygenase activity of cellulose-active lytic polysaccharide monooxygenases (LPMOs)." Nature Communications 11, no. 1 (November 13, 2020). http://dx.doi.org/10.1038/s41467-020-19561-8.
Повний текст джерелаMartin-Diaz, Javier, Carmen Paret, Eva García-Ruiz, Patricia Molina-Espeja, and Miguel Alcalde. "Shuffling the Neutral Drift of Unspecific Peroxygenase inSaccharomyces cerevisiae." Applied and Environmental Microbiology 84, no. 15 (May 18, 2018). http://dx.doi.org/10.1128/aem.00808-18.
Повний текст джерелаFreakley, Simon J., Svenja Kochius, Jacqueline van Marwijk, Caryn Fenner, Richard J. Lewis, Kai Baldenius, Sarel S. Marais, et al. "A chemo-enzymatic oxidation cascade to activate C–H bonds with in situ generated H2O2." Nature Communications 10, no. 1 (September 13, 2019). http://dx.doi.org/10.1038/s41467-019-12120-w.
Повний текст джерелаHarlington, Alix C., Keith E. Shearwin, Stephen G. Bell, and Fiona Whelan. "Efficient O-demethylation of lignin monoaromatics using the peroxygenase activity of cytochrome P450 enzymes." Chemical Communications, 2022. http://dx.doi.org/10.1039/d2cc04698a.
Повний текст джерелаLeone, Linda, Daniele D'Alonzo, Véronique Balland, Gerardo Zambrano, Marco Chino, Flavia Nastri, Ornella Maglio, Vincenzo Pavone, and Angela Lombardi. "Mn-Mimochrome VI*a: An Artificial Metalloenzyme With Peroxygenase Activity." Frontiers in Chemistry 6 (December 4, 2018). http://dx.doi.org/10.3389/fchem.2018.00590.
Повний текст джерелаMolina-Espeja, Patricia, Alejandro Beltran-Nogal, Maria Alejandra Alfuzzi, Victor Guallar, and Miguel Alcalde. "Mapping Potential Determinants of Peroxidative Activity in an Evolved Fungal Peroxygenase from Agrocybe aegerita." Frontiers in Bioengineering and Biotechnology 9 (September 14, 2021). http://dx.doi.org/10.3389/fbioe.2021.741282.
Повний текст джерелаMolina-Espeja, Patricia, Alejandro Beltran-Nogal, Maria Alejandra Alfuzzi, Victor Guallar, and Miguel Alcalde. "Corrigendum: Mapping Potential Determinants of Peroxidative Activity in an Evolved Fungal Peroxygenase From Agrocybe aegerita." Frontiers in Bioengineering and Biotechnology 9 (October 5, 2021). http://dx.doi.org/10.3389/fbioe.2021.778727.
Повний текст джерелаMolina-Espeja, Patricia, Alejandro Beltran-Nogal, Maria Alejandra Alfuzzi, Victor Guallar, and Miguel Alcalde. "Corrigendum: Mapping Potential Determinants of Peroxidative Activity in an Evolved Fungal Peroxygenase From Agrocybe aegerita." Frontiers in Bioengineering and Biotechnology 9 (October 5, 2021). http://dx.doi.org/10.3389/fbioe.2021.778727.
Повний текст джерелаMate, Diana M., Miguel A. Palomino, Patricia Molina-Espeja, Javier Martin-Diaz, and Miguel Alcalde. "Modification of the peroxygenative:peroxidative activity ratio in the unspecific peroxygenase fromAgrocybe aegeritaby structure-guided evolution." Protein Engineering Design and Selection, January 1, 2017. http://dx.doi.org/10.1093/protein/gzw073.
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