Academic literature on the topic 'Peroxygenase activity'
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Journal articles on the topic "Peroxygenase activity"
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.
Full textWillot, 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.
Full textKuo, 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.
Full textHanano, 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.
Full textNguyen, 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.
Full textNguyen, 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.
Full textMolina-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.
Full textMolina-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.
Full textQin, 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.
Full textCarballares, 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.
Full textDissertations / Theses on the topic "Peroxygenase activity"
Cirino, Patrick Carmen Arnold Frances Hamilton. "Laboratory evolution of cytochrome P450 peroxygenase activity /." Diss., Pasadena, Calif. : California Institute of Technology, 2004. http://resolver.caltech.edu/CaltechETD:etd-06062003-164310.
Full textCirino, Patrick Carmen. "Laboratory Evolution of Cytochrome P450 Peroxygenase Activity." Thesis, 2004. https://thesis.library.caltech.edu/2469/2/cirinothesis.pdf.
Full textThe ability of the cytochrome P450 heme monooxygenases to catalyze difficult oxidation reactions, often with high specificity and selectivity, makes them attractive for numerous biotechnological applications. However they are generally limited by low turnover rates and low stability, and their minimum requirements for catalysis include a cofactor as source of electrons (NAD(P)H), partner proteins for electron transfer, and dioxygen. Some P450s are capable of supporting low levels of peroxygenase activity, in which a peroxide is utilized to drive catalysis via a "shunt" pathway. This mechanism for substrate oxidation, although inefficient and not generally utilized in nature, simplifies P450 catalysis by eliminating the need for NAD(P)H.
Our goal was to engineer an efficient P450 peroxygenase which utilizes hydrogen peroxide (H₂O₂). Directed evolution is a powerful enzyme engineering methodology which mimics nature's algorithm for evolution. Enzyme libraries are generated via DNA mutagenesis or recombination techniques, and variants with improved function are isolated using an appropriate screen or selection. Using this strategy, in combination with site-directed mutagenesis, we have created P450 BM-3 heme domain variants with more than 100-fold improved H₂O₂-driven hydroxylation activity compared to wild-type, showing both an improved kcat as well as a lower Km for H₂O₂. Thermostability was also improved by directed evolution.
We have engineered a cell-free, biomimetic hydroxylase that requires only H₂O₂ to exploit the hydroxylating power of P450 BM-3. Peroxide-mediated inactivation as a result of heme destruction remains a major obstacle and presents an important enzyme engineering challenge. This research has broadened the potential applications of P450 biocatalysis by exploiting the versatility of heme-containing proteins.
Podgorski, Matthew Nathanial. "Investigation of the Mechanism of Multiple Cytochrome P450-catalysed Reactions." Thesis, 2019. http://hdl.handle.net/2440/123404.
Full textThesis (MPhil) -- University of Adelaide, School of Physical Sciences, 2020
Book chapters on the topic "Peroxygenase activity"
Coon, Minor J., Robert C. Blake, Ronald E. White, and Gerald D. Nordblom. "[27] Assays for cytochrome P-450 peroxygenase activity." In Oxygen Radicals in Biological Systems Part B: Oxygen Radicals and Antioxidants, 273–78. Elsevier, 1990. http://dx.doi.org/10.1016/0076-6879(90)86119-g.
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