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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書目名稱A Novel Heme-Thiolate Peroxygenase AaeAPO and Its Implications for C-H Activation Chemistry被引頻次




書目名稱A Novel Heme-Thiolate Peroxygenase AaeAPO and Its Implications for C-H Activation Chemistry被引頻次學科排名




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書目名稱A Novel Heme-Thiolate Peroxygenase AaeAPO and Its Implications for C-H Activation Chemistry讀者反饋




書目名稱A Novel Heme-Thiolate Peroxygenase AaeAPO and Its Implications for C-H Activation Chemistry讀者反饋學科排名

喚起

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NEX

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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卵石

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

SEEK

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