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Titlebook: A Novel Heme-Thiolate Peroxygenase AaeAPO and Its Implications for C-H Activation Chemistry; Xiaoshi Wang Book 2016 Springer International

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期刊全称A Novel Heme-Thiolate Peroxygenase AaeAPO and Its Implications for C-H Activation Chemistry
影响因子2023Xiaoshi Wang
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发行地址Nominated as an outstanding Ph.D. thesis by Princeton University, USA.Represents significant scientific advance in the field of heme-thiolate enzymes.Provides clear and colorful illustrations with ori
学科分类Springer Theses
图书封面Titlebook: A Novel Heme-Thiolate Peroxygenase AaeAPO and Its Implications for C-H Activation Chemistry;  Xiaoshi Wang Book 2016 Springer International
影响因子In this thesis, Xiaoshi Wang investigates the function and mechanism of a newly discovered heme-thiolate peroxygenase, AaeAPO. This enzyme class comes from Agrocybe aegerita and is used in the conversion of inert hydrocarbons to alcohols. Xiaoshi‘s work focuses on an extracellular P450 enzyme which is not limited in its stability and lack of solubility and therefore is relevant for widespread industrial use. The author demonstrates that the peroxygenase catalyzes a wide range of reactions. In some cases the author even describes very difficult transformations in molecules that are highly inert. Her detailed investigations provide a mechanistic framework for how the peroxygenase catalyzes such a large number of reactions. A major highlight of this thesis is the identification of key short-lived intermediates in the catalytic cycle of the peroxygenase, using rapid kinetic and spectroscopic methods, as well as the elucidation of the thermodynamic properties of these high-energy intermediates. This work adds new insight into an important class of enzymes.
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Xiaoshi WangNominated as an outstanding Ph.D. thesis by Princeton University, USA.Represents significant scientific advance in the field of heme-thiolate enzymes.Provides clear and colorful illustrations with ori
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Springer Theseshttp://image.papertrans.cn/a/image/141608.jpg
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https://doi.org/10.1007/978-0-387-49820-1utilization, high regioselectivity and stereospecificity were observed. The scope of the alkane substrates includes linear, branched and cyclic hydrocarbons, further expanding to gaseous ethane, propane and neopentane. Metabolites of several drug molecules were also analyzed and compared with P450s
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https://doi.org/10.1007/978-1-4757-3860-5 using H.O. as co-substrate with high efficiency and selectivity. It not only shows potential for practical biocatalytic application but also might provide some inspiration for designing biomimetic catalysts. In order to investigate the reaction mechanism, several radical clocks were used in this ch
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https://doi.org/10.1007/978-1-4757-2606-0 of the ferric protein with HOBr and HOCl. The rate constant for the formation of .APO-I induced by HOBr at pH 5.0, 4 °C was 7.1 × 10 M.s.. .APO-I reacts with bromide and chloride ions to regenerate the resting ferric protein. Similar measurements were made for chloroperoxidase (CPO). The rate const
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