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 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 restricted in its balance and absence of solubility and hence is proper for frequent business use. the writer demonstrates that the peroxygenase catalyzes quite a lot of reactions. every so often the writer even describes very tough variations in molecules which are hugely inert. Her unique investigations supply a mechanistic framework for the way the peroxygenase catalyzes this type of huge variety of reactions. a massive 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 houses of those high-energy intermediates. This paintings provides new perception into a huge classification of enzymes.

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Extra resources for A Novel Heme-Thiolate Peroxygenase AaeAPO and Its Implications for C-H Activation Chemistry

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Mol. Life Sci. 57, 1236–1259 (2000) 16. R. ) Cytochrome P450: Structure, Mechanism and Biochemistry, 3rd edn. pp. 1–44. Kluwer Academic/Plenum, New York (2004) 17. : Hydrocarbon hydroxylation by cytochrome P450 enzymes. Chem. Rev. 110, 932–948 (2010) 18. : Heme-thiolate proteins. Biochem. Biophys. Res. Co. 338, 404–409 (2005) 19. : Heme-containing oxygenases. Chem. Rev. 96, 2841–2887 (1996) 20. : C-H bond activation in heme proteins: the role of thiolate ligation in cytochrome P450. Curr. Opin.

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Acta. Crystallogr. F 66, 693– 698 (2010) 40. : Detection and kinetic characterization of a highly reactive heme-thiolate peroxygenase compound I. J. Am. Chem. Soc. 134, 12897–12900 (2012) 41. : Spectroscopic features of cytochrome P450 reaction intermediates. Arch. Biochem. Biophys. 507, 26–35 (2011) 42. : The use of deuterium isotope effects to probe the active site properties, mechanism of cytochrome P450-catalyzed reactions, and mechanisms of metabolically dependent toxicity. Drug Metab. Dispos.

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