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 came across 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 as a result is proper for common commercial use. the writer demonstrates that the peroxygenase catalyzes quite a lot of reactions. every so often the writer even describes very tough modifications in molecules which are hugely inert. Her certain 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 id 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 homes of those high-energy intermediates. This paintings provides new perception into a huge type of enzymes.

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

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One of the advantages of rational approaches is the relatively small variant library. This is based on the information obtained from crystal structures and mechanistic studies. Some active site volumes of proteins can be engineered to become bigger in order to increase the binding affinity of large substrate molecules. For example, cytochrome P450cam has been redesigned to be able to catalyze the regioselective aromatic hydroxylation of diphenylmethane by using a Y96A variant [92]. On the other hand, some active site volumes were down-sized with more bulky active site residues in order to fit small alkanes.

Compound I of chloroperoxidase. FEBS Lett. 305, 206–208 (1992) 70. : The use of deuterated camphor as a substrate in 1H ENDOR studies of hydroxylation by cryoreduced oxy P450cam provides new evidence of the involvement of compound I. Biochemistry 52, 667–671 (2013) 71. : Preparation and reactivity of oxoiron(IV) porphyrins. Inorg. Chem. 33, 5065–5072 (1994) 72. : Evidence for basic ferryls in cytochromes P450. J. Am. Chem. Soc. 128, 11471–11474 (2006) 73. : Oxoiron(IV) in chloroperoxidase compound II is basic: implications for P450 chemistry.

Detailed knowledge of the structural and electronic features of the intermediates are very important for a thorough understanding of the mechanism of heme-thiolate enzyme catalysts. So far, many intermediates have been detected and characterized in the catalytic cycle of porphyrin model complexes, AaeAPO, CPO and CYP enzymes by various biophysical experimental methods [41, 44, 45]. Some text books introducing physical methods used in the field of bioinorganic chemistry are referenced here [46, 47].

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