A Novel Heme-Thiolate Peroxygenase AaeAPO and Its by Xiaoshi Wang

By Xiaoshi Wang

In this thesis, Xiaoshi Wang investigates the functionality and mechanism of a newly chanced on heme-thiolate peroxygenase, AaeAPO. This enzyme classification comes from Agrocybe aegerita and is utilized in the conversion of inert hydrocarbons to alcohols. Xiaoshi's paintings makes a speciality of an extracellular P450 enzyme which isn't constrained in its balance and absence of solubility and for this reason is correct for common commercial use. the writer demonstrates that the peroxygenase catalyzes quite a lot of reactions. occasionally the writer even describes very tricky variations in molecules which are hugely inert. Her distinct investigations supply a mechanistic framework for the way the peroxygenase catalyzes this type of huge variety of reactions. an enormous spotlight of this thesis is the identity of key short-lived intermediates within the catalytic cycle of the peroxygenase, utilizing speedy kinetic and spectroscopic tools, in addition to the elucidation of the thermodynamic homes of those high-energy intermediates. This paintings provides new perception into an incredible type of enzymes.

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3 P450SPα and P450BSβ Cytochrome P450SPα (CYP152B1) from Sphingomonas paucimobilis and P450BSβ (CYP152A1) from Bacillus subtilis are CYPs classified as H2O2-dependent enzymes [33, 34]. It has been shown that P450SPα and P450BSβ catalyze fatty acid hydroxylation with high selectivity. Further, with the use of carboxylate group of the fatty acid, P450SPα and P450BSβ have been demonstrated to catalyze H2O2 dependent monooxygenation of styrene and ethylbenzene. Although crystal structures of substrate-free forms showed their lack of general acid-base residues in the active site, crystal structure of a heptanoic acid bound form of P450BSβ showed an interaction between Arg242 and the carboxylate group of heptanoic acid [35] (Fig.

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Biophys. Res. Co. 363, 954–958 (2007) 65. : Cryotrapped reaction intermediates of cytochrome P450 studied by radiolytic reduction with phosphorus-32. J. Biol. Chem. 276, 11648–11652 (2001) 66. : Evidence for compound I formation in the reaction of cytochrome-P450cam with M-chloroperbenzoic acid. Biochem. Biophys. Res. Co. 201, 1464– 1469 (1994) 67. : Cytochrome P450 compound I: capture, characterization, and C-H bond activation kinetics. Science 330, 933–937 (2010) 68. : X-ray absorption spectroscopy of chloroperoxidase compound I: Insight into the reactive intermediate of P450 chemistry.

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