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 type 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 shortage of solubility and as a result is proper for frequent commercial use. the writer demonstrates that the peroxygenase catalyzes quite a lot of reactions. in certain cases the writer even describes very tough alterations in molecules which are hugely inert. Her exact investigations offer a mechanistic framework for the way the peroxygenase catalyzes any such huge variety of reactions. a tremendous 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 classification of enzymes.

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

Sample text

New peaks are formed and corresponding to ethanol. The total turnover was about 10. The final concentration of ethanol was 6 μM calculated from an internal standard which was added when doing NMR trace and water suppressed 1H NMR of mixtures after neopentane reactions. In the right figure, the arrows pointed to two new peaks corresponding to neopentanol (2H, s and 9H, s). No neopentanol was formed in the controls without adding AaeAPO. The total turnover was about 30. In Fig. 4, the enlarged two panels show ethanol peaks (2H, q and 3H, t).

It provides information on the bond vibration modes [52]. In particular, resonance Raman spectroscopy provides bond vibrational information specifically in the vicinity of the heme. X-ray absorption fine structure (EXAFS) is a useful tool used to explore the structural information of the complexes [53]. It can provide information such as the distance between the metal-ligand, the number of ligated atoms and also the geometry. EXAFS is particularly useful if a protein crystal structure is not available.

Biochem. Biophys. Res. Co. 338, 346–354 (2005) 46. : Physical methods in bioinorganic chemistry, 1st edn. University Science Books (2000) 47. : Spectroscopic methods in bioinorganic chemistry. American Chemical Society (1998) 48. : Transient-state kinetic analysis of enzyme reaction pathways. Enzymes XX, 1– 61 (1992) 49. : Introduction to magnetic resonance. Harper and Row, New York (1967) 50. : Transition ion electron paramagnetic resonance. Oxford University Press, Oxford (1991) References 19 51.

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