By Xiaoshi Wang
In this thesis, Xiaoshi Wang investigates the functionality and mechanism of a newly stumbled on heme-thiolate peroxygenase, AaeAPO. This enzyme category comes from Agrocybe aegerita and is utilized in the conversion of inert hydrocarbons to alcohols. Xiaoshi's paintings specializes in an extracellular P450 enzyme which isn't constrained in its balance and shortage of solubility and accordingly is correct for frequent commercial use. the writer demonstrates that the peroxygenase catalyzes quite a lot of reactions. occasionally the writer even describes very tricky alterations in molecules which are hugely inert. Her specified investigations offer a mechanistic framework for the way the peroxygenase catalyzes one of these huge variety of reactions. an incredible spotlight of this thesis is the identity of key short-lived intermediates within the catalytic cycle of the peroxygenase, utilizing fast kinetic and spectroscopic equipment, in addition to the elucidation of the thermodynamic houses of those high-energy intermediates. This paintings provides new perception into a massive type of enzymes.
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Additional info for A Novel Heme-Thiolate Peroxygenase AaeAPO and Its Implications for C-H Activation Chemistry
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2 Chloroperoxidase (CPO) CPO from Caldariomyces fumugo was ﬁrst discovered by Clutterbuck and coworkers in 1940 and was found to mediate the chlorination of β-ketoadipic acid . The isolated enzyme was found to be highly glycosylated with a molecular 4 1 Hydrocarbon Oxygenation by Heme-Thiolate Enzymes Fig. 2 Alkane hydroxylation reactions catalyzed by CPO weight of about 42 kDa . 2). Besides the one-electron oxidations catalyzed by most of the peroxidases and halogenation reactions, CPO is also able to catalyze two-electron oxidations, such as oxygen atom transfer reactions, although the efﬁciency is much lower than CYPs .
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